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ORNL protein analysis investigates marine worm community
Date:5/9/2012

combination of genomics and proteomics can also help explain apparent redundancies in a system where several organisms appear at first glance to perform the same function.

"One of the key questions in metagenomic analyses of complex symbiotic consortia, including those of the human gut, is why there is so much functional redundancy," said lead author Nicole Dubilier of the Max Planck Institute for Marine Microbiology. "Our metaproteomic analyses of the bacteria found in O. algarvensis indicate functional differences in the metabolism of two symbionts despite their genetic similarities. This appears to be a common theme in microbial communities."

Metaproteomics provided indirect evidence for the research team's hypotheses about the worm community's metabolism, such as the potential use of hydrogen and carbon monoxide as energy sources. VerBerkmoes adds that while their analysis rapidly provided a broad overview of the system, the techniques do not confirm the specifics of individual protein behavior or function, which must be established via further direct biochemical studies.

The research is published as "Metaproteomics of a gutless marine worm and its symbiotic microbial community reveal unusual pathways for carbon and energy use." Coauthors include ORNL's Jacque Young, Yun-Juan Chang and Manesh Shah, and researchers from the Max Planck Institute for Marine Microbiology, the University of Greifswald, the University of Freiburg, the Institute of Marine Biotechnology in Greifswald, and the HYDRA Institute for Marine Sciences. The project was lead by Manuel Kleiner and Nicole Dubilier from the Max Planck Institute for Marine Microbiology.


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Contact: Morgan McCorkle
mccorkleml@ornl.gov
865-574-7308
DOE/Oak Ridge National Laboratory
Source:Eurekalert

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Applications include ELISA, immunochemistry, and Western blotting. Working Concentrations: ELISA: 0.005-0.05 U/ml, immunohisto/cytochemistry: 0.25-0.5 U/ml, Western blot: 0.1-0.25 U/ml....
Poly A Polymerase catalyzes the addition of AMP to the 3' hydroxyl terminus of RNA. Poly A Polymerase can add poly(C) and poly(U) to RNA but does so with much-reduced efficiency....
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