The psychrophilic lifestyle as revealed by the genome sequence of Colwellia psychrerythraea 34H through genomic and proteomic analyses.

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TitleThe psychrophilic lifestyle as revealed by the genome sequence of Colwellia psychrerythraea 34H through genomic and proteomic analyses.
Publication TypeJournal Article
Year of Publication2005
AuthorsMethé, BA, Nelson, KE, Deming, JW, Momen, B, Melamud, E, Zhang, X, Moult, J, Madupu, R, Nelson, WC, Dodson, RJ, Brinkac, LM, Daugherty, SC, Durkin, AS, DeBoy, RT, Kolonay, JF, Sullivan, SA, Zhou, L, Davidsen, TM, Wu, M, Huston, AL, Lewis, M, Weaver, B, Weidman, JF, Khouri, H, Utterback, TR, Feldblyum, TV, Fraser, CM
JournalProc Natl Acad Sci U S A
Volume102
Issue31
Pagination10913-8
Date Published2005 Aug 2
ISSN0027-8424
KeywordsAmino Acids, Bacterial Proteins, Carbon, Cold Climate, DNA, Bacterial, Energy Metabolism, Gammaproteobacteria, Genome, Bacterial, Genomics, Marine Biology, Membrane Fluidity, Models, Biological, Molecular Sequence Data, Nitrogen, Proteomics, Species Specificity
Abstract

The completion of the 5,373,180-bp genome sequence of the marine psychrophilic bacterium Colwellia psychrerythraea 34H, a model for the study of life in permanently cold environments, reveals capabilities important to carbon and nutrient cycling, bioremediation, production of secondary metabolites, and cold-adapted enzymes. From a genomic perspective, cold adaptation is suggested in several broad categories involving changes to the cell membrane fluidity, uptake and synthesis of compounds conferring cryotolerance, and strategies to overcome temperature-dependent barriers to carbon uptake. Modeling of three-dimensional protein homology from bacteria representing a range of optimal growth temperatures suggests changes to proteome composition that may enhance enzyme effectiveness at low temperatures. Comparative genome analyses suggest that the psychrophilic lifestyle is most likely conferred not by a unique set of genes but by a collection of synergistic changes in overall genome content and amino acid composition.

DOI10.1073/pnas.0504766102
Alternate JournalProc. Natl. Acad. Sci. U.S.A.
PubMed ID16043709
PubMed Central IDPMC1180510