Scientists unlock mystery of how the 22nd amino acid is produced

The most recently discovered amino acid, pyrrolysine, is produced by a series of just three chemical reactions with a single precursor – the amino acid lysine, according to new research.

Scientists at Ohio State University used mass spectrometry and a series of experiments to discover how cells make the amino acid, a process that until now had been unknown.
They confirmed that pyrrolysine is made from enzymatic reactions with two lysine molecules – a surprising finding, given that some portions of its structure suggested to researchers that it might have more complex origins.
The research is published in the March 31 issue of the journal Nature.
Pyrrolysine is rare and so far is known to exist in about a dozen organisms. But its discovery in 2002 as a genetically encoded amino acid in methane-producing microbes raised new questions about the evolution of the genetic code. Pyrrolysine is among 22 amino acids that are used to create proteins from the information stored in genes. Proteins are essential to all life and perform most of the work inside cells.
This information about how it is produced – its biosynthetic pathway – offers a more complete understanding of how amino acids are made. And because of its rarity, this molecule is emerging as a handy tool for manipulating proteins in biomedical research. With its production mechanism identified, scientists can use that information to devise ways to mass-produce similar or identical synthetic molecules for a variety of research purposes.
The Ohio State scientists had a genuine "ah-ha" moment over the course of the study. As part of their experimentation, they combined lysine with one other amino acid and some enzymes and expected this to produce what is called an intermediate – essentially, a piece of an amino acid that is generated in the biosynthesis process.
They had labeled the lysine so it would appear heavier than normal when observed using mass spectrometry. But one signal produced by the instrumentation had a much different mass than could be attributed to the intermediate.
"We weren't seeing this weird molecule made from two different amino acids that we were expecting. We were seeing the regular pyrrolysine molecule and all of it was coming from lysine. Every bit of it," said Joseph Krzycki, professor of microbiology at Ohio State and senior author of the study. "That was the only way we saw pyrrolysine, and all of it was labeled with lysine. That's the basic observation here. And it's a real surprise."
The finding that lysine was the only precursor was a surprise because the production process ended up being so simple – even though arriving at it was not a simple task, partly because some of the chemical reactions had never been observed before.
"What amazes me about the entire chemical pathway is that you need only three enzymes and two molecules of the same thing that together make one complete molecule that looks completely different from what you started with," said Marsha Gaston, first author of the paper and a doctoral student in microbiology. "You have one portion that looks exactly like the precursor, but then you have another portion that enzymes are able to re-arrange in a way that is completely unique and never seen before."
Mass spectrometry, an analytic technique that enables precision in determining the mass of particles, ended up being critical to the discoveries, Krzycki noted. Liwen Zhang and Kari Green-Church of Ohio State's Campus Chemical Instrument Center/Mass Spectrometry and Proteomics Facility are additional co-authors of the study.
Krzycki led one of the two teams of Ohio State researchers that discovered pyrrolysine in 2002. The teams have since synthesized the amino acid and shown how bacteria incorporate it into proteins.
"That left some big questions unanswered: How do you make pyrrolysine? Where does it come from? What metabolic pathways does it come off of? Because it's got to be generated within the cell that uses it," Krzycki said.
The chemical shape of pyrrolysine offered some clues. Its carbon skeleton resembles that of lysine. But it also has an unusual ring on one end, and a methyl group attached to it, which for researchers raised questions about its origin.
The researchers also knew from their previous work that three genes are required to generate the instructions for the assembly of proteins that contain pyrrolysine – pylB, pylC and pylD. So the enzymes produced by those three genes had to have a role in creation of the amino acid. Finally, previous attempts by other researchers to define its biosynthesis suggested that another amino acid, D-ornithine, was involved in pyrrolysine's production.
So Krzycki and his colleagues set out to test that theory. Conducting all of their experiments in a strain of E. coli bacteria, commonly used to test biological functions, they combined lysine and D-ornithine molecules.
They found that this didn't make pyrrolysine, but rather a molecule like pyrrolysine that was missing a key part; however, this molecule turned out not to be converted to pyrrolysine. This molecule also was formed without the involvement of pylB – a gene that could not be left out of the process that actually makes pyrrolysine.
With the mass spectrometry instead identifying lysine as the only precursor to pyrrolysine, the researchers then used genetics, mass spectrometry of intermediates and deduction to determine the order of enzymatic reactions that converted two lysine molecules into the pyrrolysine amino acid.
They determined that the sequence of events matched the alphabetical order of the three involved enzymes: PylB uses lysine to make a D-ornithine-like intermediate, PylC joins the two lysine molecules together, and that feeds a reaction involving PylD that results in the formation of pyrrolysine. The reactions showed how the ring on pyrrolysine's end, its major identifying characteristic, is formed.
"If you splay out the pyrrolysine molecule, you can recognize that in fact it looks a lot like lysine, except that to get to this ring, you have to make the second molecule one carbon unit shorter," Krzycki said. "The lysine goes through a type of enzymatic reaction called a mutase reaction, where the carbon skeleton is rearranged to make this shorter molecule, which is like D-ornithine, but with one extra carbon now hanging off the chain in a new place. That's what one of our pyrrolysine biosynethetic enzymes, PylB, is doing."
Krzycki noted that this finding will add fuel to discussions of how the genetic code evolved. For example, the co-evolutionary theory suggests that amino acids arising from a common precursor have similar codon assignments. Codons are three-letter "words" identifying the bases that DNA uses to specify particular amino acids as building blocks of proteins. Normally, codons signal the start or end of a protein, or a particular amino acid used to construct it.
"For the scientists who are devoted to exploring how the genetic code evolved, our data provides new insights that can feed the various theories for how the code evolved; the co-evolutionary theory is just one such example," Krzycki said.
The finding that pyrrolysine derives entirely from lysine means that pyrrolysine is part of the aspartic acid family in bacteria and Archaea, a group of single-cell microorganisms that are similar to bacteria in size and shape, but with a different evolutionary history. The microbes known to contain pyrrolysine are in the Archaea domain, and are able to convert a common class of compounds – the methylamines – into methane gas.

Being in a Good Mood May Lead to Poor Memory

ScienceDaily (Mar. 30, 2011) — Most people have had trouble remembering something they just heard. Now, a University of Missouri researcher found that forgetfulness may have something to do with being in a good mood. Elizabeth Martin, a doctoral student of psychology in the College of Arts and Science, has found that being in a good mood decreases your working memory capacity.

"Working memory, for example, is the ability to recall items in a conversation as you are having it," Martin said. "This explains why you might not be able to remember a phone number you get at a party when you are having a good time. This research is the first to show that positive mood can negatively impact working memory storage capacity. This shows that although systems in the brain are connected, it is possible to affect one process but not others."
Researchers gauged study participants' mood before and after showing them a video clip. Some participants were shown a segment of a stand-up comedy routine, while others watched an instructional video on how to install flooring. Following the videos, those that viewed the comedy routine were in significantly better moods after viewing the video, while the mood of those that viewed the flooring video had not changed.
After watching the videos, both groups completed a memory test. This test provides several numbers to a participant through headphones at a rate of four numbers per second. After the recording stopped, participants were asked to recall the last six numbers in order. Those that watched the comedy routine and were in a better mood performed significantly worse on the task.
"While working memory storage is decreased, being in a good mood is not all bad," Martin said. "Being in a good mood has been shown to increase creative problem-solving skills and other aspects of thinking." Martin said future research should analyze the impact of mood on working memory storage capacity in real life situations, such as a classroom setting.
The study was published earlier this year in the journal Cognition and Emotion. The research was funded by grants awarded to research advisor Associate Professor John Kerns from the National Institute of Mental Health, the National Institute of Drug Abuse and a grant from the MU Research Board.

Through the Looking Glass: Research Into Brain's Ability to Understand Mirror-Image Words Sheds Light on Dyslexia

ScienceDaily (Mar. 31, 2011) — Human beings understand words reflected in a mirror without thinking about it, just like those written normally, at least for a few instants. Researchers from the Basque Centre on Cognition, Brain and Languages (Spain) have shown this in a study that could also help to increase our understanding of the phenomenon of dyslexia.

Most people can read texts reflected in a mirror slowly and with some effort, but a team of scientists from the Basque Centre on Cognition, Brain and Language (BCBL) has shown for the first time that we can mentally turn these images around and understand them automatically and unconsciously, at least for a few instants.
"At a very early processing stage, between 150 and 250 milliseconds, the visual system completely rotates the words reflected in the mirror and recognises them," says Jon Andoni Duñabeitia, lead author of the study, "although the brain then immediately detects that this is not the correct order and 'remembers' that it should not process them in this way."
In order to carry out this study, which has been published in the journal NeuroImage, the researchers used electrodes to monitor the brain activity of 27 participants while carrying out two experiments in front of a computer screen.
In the first, the participants were shown words with some of the letters and other information rotated for 50 milliseconds (an imperceptible flash, which is processed by the brain); while in the second case the entire word in the mirror was rotated (for example HTUOM INSTEAD OF MOUTH).
The results of the encephalogram showed in both cases that, at between 150 and 250 milliseconds, the brain's response upon seeing the words as reflected in the mirror was the same as when they are read normally.
Better understanding of dyslexia
"These results open a new avenue for studying the effects of involuntary rotation of letters and words in individuals with reading difficulties (dyslexia) and writing problems (dysgrafia)," Duñabeitia explains.
The researcher gives reassurance to parents who worry when their children reverse their letters when they start to write: "This is the direct result of the mirror rotation property of the visual system." In fact, it is common for children to start to write this way until they learn the "established" forms at school.
"Now we know that rotating letters is not a problem that is exclusive to some dyslexics, since everybody often does this in a natural and unconscious way, but what we need to understand is why people who can read normally can inhibit this, while others with difficulties in reading and writing cannot, confusing 'b' for 'd', for example," explains Duñabeitia.
The scientific community has yet to discover how reading, a skill that is learnt relatively late in human development, can inhibit mental rotation in a mirror, a visual capacity that is common to many animals.
"A tiger is a tiger on the right side and the left side, but a word read in the mirror loses its meaning -- although now we know that it is not as incomprehensible for our visual system as we thought, because it is capable of processing it as if it were correct," the researcher concludes.

Nanodisk gene therapy

One of the challenges of gene therapy - a set of methodologies aimed at treating several nucleic acid diseases (DNA or RNA) - is to assure that this material arrives directly to the nucleus of the cell without losing a substantial amount along the way and without producing any undesired side effects. With this aim, scientists experiment with the use of different types of vectors, molecules capable of transporting genetic material to the correct place. Presently, natural "deactivated" viruses are the most commonly used vectors in clinical trials, their side effects however often limit therapeutic application.

One of the most promising alternatives in this field is the use of artificial viruses. These viruses can be constructed through genetic engineering by assembling minute protein structures made up of peptides, the building blocks of proteins.

The team of scientists, led by Antonio Villaverde, lecturer of the Department of Genetics and Microbiology, researcher at the UAB Institute of Biotechnology and Biomedicine and of the Biomedical Research Networking Center in Bioengineering, Biomaterials and Nanomedicine (CIBER-BBN), demonstrated that the peptide R9, formed by a specific type of amino-acid (arginine), can encapsulate genetic material, assemble itself with other identical molecules to form nanoparticles and enter directly into the cell nucleus to release the material it contains. The nanoparticles have the shape of a disk, with a diameter measuring 20 nanometres and a height of 3 nm.

The study was published recently in the journals Biomaterials and Nanomedicine and describes how scientists studied the performance of R9 nanodisks in the interior of the cells using confocal microscopy techniques provided by the UAB Microscopy Service and applied by Dr Mònica Roldán. The images show that once the cell membrane is passed, particles travel directly to the nucleus at a rate of 0.0044 micrometres per second, ten times faster than if they dispersed passively in the interior. Nanoparticles accumulate in the interior of the nucleus and not in the cytoplasm - the thick liquid between the cell membrane and nucleus - and therefore increase their level of effectiveness. One of the photos was selected by the journal Biomaterials as one of the 12 images of the year 2010.

Participating in this discovery were researchers from the Institute of Material Science of Barcelona (ICMAB-CSIC), the Catalan Institute for Research and Advanced Studies (ICREA), and the Technical University of Catalonia. The discovery represents a new category of nanoparticles offering therapeutic benefits. According to Dr Esther Vázquez, director of the project, "nanodisks assemble automatically, move rapidly, remain stable and travel to the interior of the nucleus. This makes them a promising tool as a prototype for the safe administration of nucleic acids and functional proteins."

First 'Nano' Gene Therapy Treatments to Target Cancer Cells

Image Credit: Genetics and Health

Cancer Research UK scientists have for the first time developed a treatment that transports 'tumour busting' genes selectively to cancer cells, according to a study published online in Cancer Research *.
Using nanotechnology, the researchers were able to package anti-cancer genes in very small particles that directed the treatment selectively to tumours in mice so that it was only taken up by cancer cells, leaving healthy cells unharmed.
Once taken up by cancer cells, the genes enclosed in the nanoparticles force the cell to produce proteins that can kill the cancer.
In this study the cells were forced to make a protein which was then visible in whole-body scans of the mice revealing that healthy cells were not affected by the treatment.
Previous studies showed that the type of gene therapy used in this study can shrink tumours and even cure around 80 per cent of the mice given the treatment.
This type of technology is particularly relevant for people with cancers that are inoperable because they are close to vital organs, like the brain or lungs. These cancers are often associated with poor survival.
Now scientists have found a particle that can be used to selectively target cancer cells, they hope nanotechnology can be extended to treat cancer that has spread.
Study author Cancer Research UK's Dr Andreas Schatzlein, based at the School of Pharmacy in London, said: "Gene therapy has a great potential to create safe and effective cancer treatments but getting the genes into cancer cells remains one of the big challenges in this area. This is the first time that nanoparticles have been shown to target tumours in such a selective way, and this is an exciting step forward in the field.
"Once inside the cell, the gene enclosed in the particle recognises the cancerous environment and switches on. The result is toxic, but only to the offending cells, leaving healthy tissue unaffected.
"We hope this therapy will be used to treat cancer patients in clinical trials in a couple of years."
Traditional chemotherapy indiscriminately kills cells in the affected area of the body, which can cause side effects like fatigue, hair loss or nausea. It is hoped that gene therapy will have fewer associated side effects by targeting cancer cells.
Dr Lesley Walker, Cancer Research UK 's director of cancer information, said: "These results are encouraging, and we look forward to seeing if this method can be used to treat cancer in people. Gene therapy is an exciting area of research, but targeting genetic changes to cancer cells has been a major challenge. This is the first time a solution has been proposed, so it's exciting news."

Benefits of Human Cloning

The technology of cloning gained notoriety with the creation of Dolly, the first cloned mammal. Would humans be cloned too? While there are people who believe that we are trying to play God with the development of this technology, there are surely some immense benefits of human cloning. This article will try to throw light on these benefits of human cloning technology.

By Ashwini Ambekar | Saturday, May 02, 2009

Human cloning is an assisted form of reproductive technology that can be carried out to create a newborn that is identical to a human being. The human cloning process is called nuclear transplantation. The human cloning process begins with the removal of the nucleus of the egg cell and this is replaced with a nucleus of an adult cell. The egg so reconstructed is stimulated to start dividing. On successful division a pre-implantation embryo is created and this is called blastocyst. If this blastocyst is placed within the uterus it can form a fetus and this can develop into a newborn. The individuals born through this process would have similar nuclear genes like those in the adult cells but they would not resemble the adults exactly. The advantages of human cloning or the associated benefits of this process include:

Reverse Aging and Resolving of Heart Problems

Some of the experts in this form of technology suggest that with the human cloning technology it would eventually be possible to reverse the aging process. The benefits of human cloning can be gauged from the fact that this technology can be used to aid victims of heart attack. In this healthy heart cells can be cloned and injected in areas within the heart that are damaged following the heart attack. The benefits of this can be tremendous since heart disease is the prime killer within the United States and several other developed countries.

Repair Damaged Tissue and Organs

Human cloning techniques can also be used to grow organs or repair tissues and damaged organs. Conditions like Parkinson’s, diabetes and Alzheimer’s may also be cured with this technology.

Infertility

One of the greatest human cloning benefits could be resolution of  the problem of infertility. The present treatments available for infertility problems are not as successful. These treatments involve a great deal of emotional and physical trauma to the couples and human cloning could help those suffering from infertility to have children.

Plastic Surgery

Human cloning can help in procedures such as cosmetic surgeries including breast implants. The procedure will allow for use of actual tissue in the body instead of use of foreign material such as silicone gel. Doctors may also be able to produce bones and cartilages and problems associated with the use of silicone will be removed. It may be possible for doctors to perform reconstructive surgeries on faces of individuals involved in traumatic accidents as also development of limbs for amputees.

Defective Genes

People on an average carry 8 defective genes and these genes cause certain illnesses. Human cloning can allow these problems to be eradicated. Some of the problems occurring because of these defective genes include Down’s syndrome and Tay-Sachs disease among others. So women at risk for illnesses like these could take the benefits of human cloning to ensure that their offspring do not have the genes of that disorder.

Organ Transplantation and other Illnesses

Human cloning can also be used to clone livers and used in liver transplants as well as in kidney transplants though cloning of kidneys. Human cloning could be used to clone bone marrow for individuals suffering from leukemia. This could be one of the biggest benefits of human cloning technology. In organ transplantation cloning technology may help millions of people to get a new lease of life. They will no longer need to wait for years to get a donor match and the possibility of immune response to the transplantation may also be eradicated the with cloning of organs.

Cancer

Cancer is a disease that kills millions of individuals in many countries. Scientists are still trying to understand how cells differentiate in specific tissues or why certain cells lose the differentiation. The cloning technology may actually allow a cure to be found for this dreaded disease.

Other injuries

Accidents are often responsible for leaving people handicapped. People suffering from spinal cord injuries are currently not able to recover completely. With the cloning technology medical professionals may actually be able to grow back the nerves and spinal cord again so that those who are injured can hope to lead a normal life again.

Preservation of Endangered Animals

While the cloning technology may eventually be used to benefit humans it can also be used to conserve endangered species of animals.

There are a large number ethical issues surrounding this fragile topic and many people have different opinions about the cloning technology. However the benefits of human cloning can be tremendous if this technology is properly used.

BioLogic Food Plot Tips: Porch Talk

http://www.articleswave.com/videos/biologic-food-plot-tips-porch-talk-109319981.html

Did you know Honey?

If you're looking for something different to sweeten your foods with that will have more health benefits than regular sugar, look no further than to honey. Honey is often passed over for its health benefits as people do tend to look at is as a simple carbohydrate, but as long as you're being sure to keep the portion sizes down to a moderate level, there's no reason you can't include honey in your day.
Let's take a look at some of the health benefits that this sweet liquid has to offer.
Better Blood Sugar Control
The first benefit that honey has to offer over that of regular sugar is that it appears to give users a much better blood sugar control. This is largely due to the fact that honey contains the perfect blend of glucose and fructose so it won't cause nearly as large of a blood glucose spike as some of the carbohydrates (from the fructose) will go directly into the liver cells.
It's also believed that by having the liver glycogen stores full through the consumption of honey or other fructose containing foods, you can help increase feelings of satiety in the body and therefore help reduce the chances of consuming too many calories.
Lower Levels Of Belly Fat Accumulation
Also important to note, with the fructose found in honey being directed towards the liver cells, that's going to help prevent the release of a certain hormone in the body known as cortisol, which when seen in high concentrations may promote fat build-up in the abdominal cavity.
Cortisol is largely a stress hormone that's also secreted in times of high-stress or anxiety but it's also going to be secreted when liver glycogen levels run low as well.
Acts As A Cough Suppressant
Finally, one last interesting benefit of honey is that it can act as a cough suppressant in the body and work better in young children than traditional cough syrup. Stirring a tablespoon of honey into a mug of hot tea can be the perfect way to sooth a sore throat and help to reduce the instance of coughing in young children.
As an additional benefit as most of those who are sick are not taking in sufficient calories, the added calorie boost from honey will provide their body with energy to fight off the cold.
So instead of putting in another spoonful of sugar into your cup of coffee or tea, try some honey instead. It'll offer numerous health benefits and you'll still get that great sweet taste that you enjoy.

First Preliminary Profile of Proteins in Bed Bugs' Saliva

The saliva of bed bugs contains unique substances that could lead to vaccines to prevent allergic responses to the bugs' bite. This 2006 photograph depicts an oblique-dorsal view of a bedbug nymph, Cimex lectularius, as it was in the process of ingesting a blood meal from the arm of a "voluntary" human host. (Credit: Piotr Naskrecki, via CDC Public Health Image Library)

In the report, Jose Ribeiro and colleagues point out that bed bugs have made reappearances in New York City, London, and other areas, sparking increased scientific interest in the allergic responses associated with their bites. Bed bugs belong to a group of insects that feed on blood throughout their lives and have been doing so successfully for at least 250 million years. That success depends in large part on proteins in their saliva, substances that make the victim's blood vessels dilate (for a better flow of blood), inhibit clotting, and prevent immediate pain and itching that might evoke a lethal slap.

Using adult bed bugs from a government-maintained colony, the scientists removed salivary glands from male and female bugs, and analyzed the proteins to find unique enzymes that characterize the saliva profile of the bug. The substances could also offer insight into how insects evolved to a blood diet. "Independent of their function, these proteins may also be used for immune detection of humans and animals to bed bug exposure, or as part of desensitization vaccines," the report says.

Bug With Bifocals Baffles Biologists

University of Cincinnati researchers are reporting on the discovery of a bug with bifocals -- such an amazing finding that it initially had the researchers questioning whether they could believe their own eyes. (Credit: Elke Buschbeck)

ScienceDaily (Aug. 24, 2010) — University of Cincinnati researchers are reporting on the discovery of a bug with bifocals -- such an amazing finding that it initially had the researchers questioning whether they could believe their own eyes.

"To the best of our knowledge, this is the first demonstration of truly bifocal lenses in the extant animal kingdom," the researchers state in the Aug. 24 cover feature of the life-science journal Current Biology.

The new article is an exploration of two eyes of the larvae of the sunburst diving beetle (Thermonectus marmoratus). The two eyes have the bifocal lens, which the researchers have found in four of the larvae's 12 eyes, says researcher Elke K. Buschbeck, a UC associate professor of biology.

The article explains that using two retinas and two distinct focal planes that are substantially separated, the larvae can more efficiently use these bifocals, compared with the glasses that humans wear, to switch their vision from up-close to distance -- the better to see and catch their prey, with their favorite food being mosquito larvae.

"In addition, we think that within the principle eyes, separate images of the same object could be focused on each of the two retinas, allowing each eye to function as 'two eyes in one,'" the researchers reveal in the article. The tubular-shaped eyes with the bifocals allow them to efficiently focus onto their two retinas, says Annette Stowasser, a UC biology doctoral student and first author on the paper.

The discovery was made in Buschbeck's lab and was supported by her National Science Foundation CAREER award to recognize the research and teaching talent of young faculty. "We're hoping this discovery could hold implications for humans, pending possible future research in biomedical engineering," Buschbeck says.

"The discovery could also have uses for any imaging technology," adds Stowasser.

Bugs with Bifocals

The sunburst diving beetle larvae that was studied typically live in creeks and streams around Arizona and the western United States. It's classified as a holometabolous insect -- the group of insects that morph into something completely different from how they originated -- like the caterpillar/moth or the maggot/fly. The larvae of these beetles have the bifocal lens. They lose these intricate lenses when they become a beetle.

Researchers Couldn't Believe Their Eyes

As the researchers zeroed in on how the multiple eyes of this insect worked, they did even more research to try to disprove what they saw. They first used a microscope to look through the lenses of the two eyes detailed in the research article. They saw how the lens could make a second image grow sharper -- something that could only happen with a bifocal. "It was my first research project, and I seriously thought I made a mistake, and then we did additional research to try to kill the hypothesis," says Stowasser. However, their findings were confirmed with more research in addition to observing the operation of the lens and the two focal planes via a microscope. They saw the bifocal again when they used a method to project a narrow light beam through the lens. "Our findings can only be explained by a truly bifocal lens," write the researchers.

Contributing researchers included Alexandra Rapaport, a UC undergraduate neuroscience major; John E. Layne, UC assistant professor of biological science; and Randy C. Morgan, Invertebrate Conservation program manager for the Cincinnati Zoo & Botanical Garden.

The UC research was supported by Buschbeck's $805,000 CAREER award from the National Science Foundation, which was awarded in 2005. The Cincinnati Zoo and Botanical Garden provided the original population of sunburst diving beetles for the research.

Titanic Being Eaten by Destructive Bacteria

A rust stain may be all that will remain of the RMS Titanic in 15 to 20 years, according to new research into the submerged ocean liner wreck.

Working at a depth of over two miles, a never-before-seen bacterial species is devouring the hull of the so-called "unsinkable ship" on the Atlantic seabed where it sank on April 15, 1912, killing 1,517 people.

Named Halomonas titanicae, the bacterium was isolated from samples of so-called rusticles present on the wreck.

These dark orange structures look like icicles but are made up of rust.

"The isolate was obtained from rusticle samples collected during the Akademic Keldysh expedition in 1991, at the site of the wreck," Canadian and Spanish researchers write in the latest issue of the International Journal of Systematic and Evolutionary Microbiology published on Dec. 8.

Removed from the hull using the articulated arm of the Mir 2 robotic submersible, the rusticles were transferred to plastic collection bags and transported aseptically to the surface to be analyzed.

Using DNA technology, the researchers discovered that the rusticles were formed by a combination of 27 different strains of bacteria.

Among the bacteria feasting on the Titanic, there was a brand new member of the salt-loving Halomonas genus.

"We don't know yet whether Halomonas titanicae arrived aboard the RMS Titanic before or after it sank," said lead researcher Henrietta Mann, at Dalhousie University, Halifax, Canada.

Able to adhere to steel surfaces, the new species has led to the formation of knob-like mounds of corrosion. Covered with such rust mounds, the wreck of the Titanic is at risk of disintegrating into dust, as the porous rusticles eventually dissolve into fine powder.

Discovered in 1985, about two miles below the ocean surface and some 329 miles southeast of Newfoundland, Canada, the wreck of the Titanic has been progressively deteriorating.

Originally made up of 50,000 tons of iron, the ship has dramatically split apart: the stern and the bow lie some 2,000 feet apart in opposite directions.

While potentially dangerous to underwater metal structures like shipwrecks, as well as offshore oil and gas pipelines, the newly discovered species could also offer positive applications for industry.

"The new specie of bacteria plays a significant part in the recycling of iron structures in deep ocean. It could be useful in the disposal old naval and merchant ships and oil rigs," Mann told Discovery News.

According to Bhavleen Kaur, science educator at the Ontario Science Centre, Toronto, Canada, finding a new species is important, but even more exciting is the environment found in the rusticles.

"Out of the consortium of microbes, whose actions are responsible for the formation of rusticles on the Titanic wreck, Halomonas titanicae is the first to be fully characterized and named. How many more novel species are living within the rusticles? How did they get there or did they evolve within this artificially created mini-ecosystem?...These microbes can be an addition to the tool kit when we carry further investigations into corrosive processes," Kaur told Discovery News.

Where did all the sparrows go?

The sparrows have disappeared completely from the cities at least four years ago in Britain, as mobile phones grew in popularity. Third generation (3G) mobile phones were introduced in 2003, and there were over 65 million users in the UK by the end of 2005, more phones than people. Did mobile phone transmitters cause the sparrows to disappear ?

Scientists at the Research Institute for Nature and Forests in Brussels, Belgium, have produced the first evidence that mobile phone base stations are affecting the reproductive behaviour of wild sparrows. This finding comes as mobile phones are held suspect in the massive collapse of bee colonies all over the United States and Europe (Mobile Phones and Vanishing bees)

Joris Everaert and Dirk Bauwens wanted to know if the low intensity microwave radiation from mobile phone base stations has any effect on the number of house sparrows during the breeding season. They identified 150 locations distributed over six residential districts in Gent, Sint and Niklaas in the province of East Flanders, where they counted the number of male house sparrows and measured the strength of electromagnetic radiation from base stations.

The study areas were similar, with abundant hedges, bushes, and other vegetation between the houses, and one or more GSM (Global System for Mobile Communications) base stations nearby. All locations were along small roads within the residential areas and at variable distances from the nearest GSM (mean 352 m, range 91-903 m, about 90 percent at 100-600 m). On days when the weather was favourable, so male sparrows would be out singing, the researchers went to each location between 7 and 11 am, and using binoculars, counted the number of male sparrows within a radius of about 30 m for a period of five minutes.

Simultaneously, they measured the maximum value of the electric field strength (in V/m) from the GSM 900 MHz and GSM 1800 MHz base station antennas during 2 minutes for each frequency band, using a portable calibrated high-frequency spectrum analyser.

Everaert and Bauwens found that the number of house sparrow males varied between zero and four at the different locations. The measured electric field strengths were seldom higher than 1V/m, and most often well below that value. Nevertheless, the spatial variation in the number of house sparrow males was negatively and highly significantly correlated to the strength of electric fields from both the 900 and 1800 MHz frequency bands and from the sum of these bands. This negative correlation was very similar within each of the six districts, despite differences in both the number of birds and radiation levels.

Fewer house sparrow males were seen at locations within relatively high electric field strengths of GSM base stations. For example, the mean number of male sparrows varied from 1.9 at the combined field intensity of 0.13 V/m to 0.8 at a combined field intensity of 0.247 V/m.

The results, though preliminary, do support the hypothesis that long-term exposure to higher levels of radiation negatively affects the abundance or behaviour of house sparrows in the wild. Fewer males singing would mean less breeding success.

The Monarch butterfly (Danaus plexippus)

The Monarch butterfly (Danaus plexippus) is a milkweed butterfly (subfamily Danainae), in the family Nymphalidae. It is perhaps the best known of all North American butterflies. Since the 19th century, it has been found in New Zealand, and in Australia since 1871 where it is called the Wanderer. Europe it is resident in the Canary Islands, the Azores, and Madeira, and is found as an occasional migrant in Western Europe. Its wings feature an easily recognizable orange and black pattern, with a wingspan of 8.9–10.2 centimetres (3½–4 in). (The Viceroy butterfly has a similar size, color, and pattern, but can be distinguished by an extra black stripe across the hind wing.) Female Monarchs have darker veins on their wings, and the males have a spot called the "androconium" in the center of each hind wing from which pheromones are released. Males are also slightly larger.

The Monarch is famous for its southward migration and northward return in summer in the Americas which spans the life of three to four generations of the butterfly.

Kiwa hirsuta - the blind fuzzy white lobster

Posted in crustacean by Critter Lover on the March 8th, 2006

Okay, it’s not actually a lobster but that’s how it’s being described.

It’s so unique that a new family (Kiwaida) and genus was created for it.

Here are links to a few sites reporting on the discovery:

The name of the new family and genus refers to Kiwa, the goddess of the shellfish in Polynesian mythology.

The species name K. hirsuta comes from Latin and means hairy!

Kingdom: Animalia
Phylum: Arthropoda
Subphylum: Crustacea
Class: Malacostraca
Order: Decapoda
Suborder: Pleocyemata
Infraorder: Anomura
Superfamily: Galatheoidea
Family: Kiwaidae
Genus: Kiwa

NASA's New Life Form a Boon for Clean Energy, Toxic Waste Cleanup

by Brian Merchant, Brooklyn, New York

Image: NASA

The intertubes were abuzz with the big news from NASA yesterday: Researchers announced they discovered a new kind of life that rearranges all our assumptions about life as we know it (but first they had to apologize that no, it wasn't an alien). This life form, a microbe that substitutes phosphate (heretofore a building block of all life on earth) with toxic arsenic, is truly an amazing discovery. Even more amazing is that the horizon-expanding discovery could be a huge boon to both clean energy and toxic waste cleanup -- it could change both sectors in some pretty revolutionary ways.