IN THIS ISSUE .
. .
March 18, 2009
- Cool Image: Genetic Patchworks
- Flu 'Supermantibody'
- Sirtuin Brings Stressed Protein Into the Fold
- Detecting Chemicals Within and Around Us
- Creative Chemistry Could Lead to New Drugs, Tools
Check out the Biomedical Beat Cool Image Gallery.
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Cool Image: Genetic Patchworks
Each point in these colorful patchworks represents the correlation between two sleep-associated genes in fruit flies. Vibrant reds and oranges represent high and intermediate degrees of association between the genes, respectively. Genes in these areas show similar activity patterns in different fly lines. Cool blues represent gene pairs where one partner's activity is high and the other's is low. The green areas show pairs with activities that are not correlated. These quilt-like depictions help illustrate a recent finding that genes act in teams to influence sleep patterns. Courtesy of geneticists Susan Harbison and Trudy Mackay, North Carolina State University.
Full story
Mackay lab
Article abstract (from the February 22 online issue of Nature Genetics)
Flu 'Supermantibody'
They call it a super antibody—an infection-fighting protein that recognizes seasonal and pandemic influenza viruses. Researchers had previously identified the antibody, CR6261. To understand how the protein responded to different flu viruses, a team led by structural biologist Ian Wilson of The Scripps Research Institute solved the structure of it bound to two different mushroom-shaped viral proteins called hemagglutinin. Most flu antibodies target the mushroom cap, but CR6261 latched on to the stalk—an area that the researchers found is highly conserved among many influenza viruses. This discovery is good news for researchers who hope to design a vaccine offering lifelong protection against a range of flu viruses.
NIH's National Institute of Allergy and Infectious Diseases and National Cancer Institute also supported this work.
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Wilson lab
Article abstract (from the February 26 online issue of Science)
Sirtuin Brings Stressed Protein Into the Fold
A molecular chaperone (yellow) envelops a misfolded protein (blue) in the center of this human cell. Courtesy of Richard Morimoto.
High res. image
(60 KB GIF)
Experiments in animals and people have shown that the protein sirtuin is linked with enhancing lifespan by keeping cells healthy. Now, molecular biologist Richard Morimoto of Northwestern University has found that sirtuin helps ensure that important cell proteins are folded properly. He and coworkers in Finland discovered that sirtuin, in response to cell stress, hooks up with a molecular "chaperone" that both senses and prevents further protein damage. Because many diseases of aging involve protein folding problems, the latest work may point to new diagnostic and treatment approaches for Alzheimer's, Parkinson's, Huntington's and adult-onset diabetes.
NIH's National Institute on Aging also supported this work.
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Morimoto lab
Article abstract (from the February 20 issue of Science)
Detecting Chemicals Within and Around Us
RNA molecules could help measure chemicals in our bodies and the environment.
Harnessing a molecule found in every living organism, scientists at The Scripps Research Institute created a powerful way to detect the presence and quantity of countless substances. The technique, which relies on tailor-made, self-replicating RNA molecules, could be used as a diagnostic tool to measure specific proteins or drugs in the body or chemicals in the environment. The scientists, Bianca Lam and Gerald Joyce, used the technique to accomplish a task that is difficult with current techniques: measuring the level of an asthma drug that can be toxic at high concentrations and distinguishing it from a very similar chemical, caffeine.
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Joyce lab
Article abstract (from the February 22 online issue of Nature Biotechnology)
Creative Chemistry Could Lead to New Drugs, Tools
Scientists devised a way to connect chemical groups to specific areas on proteins. Courtesy of Judith Stoffer.
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Biological chemist Carolyn Bertozzi and her colleagues at Lawrence Berkeley National Laboratory and the University of California-Berkeley have developed what promises to be a fast, easy-to-use tool for creating new drugs and other useful molecules. The work accomplishes the long-sought goal of adding a chemical tag to a selected spot on a protein in mammalian cells. The tag, called an aldehyde, acts like a trailer hitch that facilitates the addition of various other compounds to the protein. This gives the protein desired qualities, such as a longer life-span or drug-like capabilities. After Bertozzi and a coworker successfully tagged several different proteins, they launched a company to commercialize the technique.
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Bertozzi lab
Article abstract (from the February 6 online issue of PNAS)