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Approaches to assigning protein function in E. coli
Author(s) -
Armstrong Richard N.
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.204.1
Subject(s) - escherichia coli , function (biology) , transferase , gene , context (archaeology) , biology , glutathione s transferase , computational biology , glutathione , genome , genetics , biochemistry , enzyme , paleontology
Understanding the functional genomics of organisms has emerged as a fundamental challenge of biochemistry. Almost 40% of the genes in one of the best‐understood organisms in the biosphere, Escherichia coli , still have no experimentally verified function. In this work the challenge of, and criteria for, assigning protein function in the context of the glutathione (GSH) transferase paralogues encoded in the E. coli genome will be discussed. The E. coli genome harbors eight genes encoding canonical GSH transferase homologues including YliJ, YncG, Gst YfcF, YfcG, YghU, SspA and YibF. Only one of these gene products (SspA) has a well‐defined function. The structures and possible functions of GSH transferase homologues, YfcG, YghU and YghU, will be discussed with respect to GSH and glutathionylspermidine homeostasis in E. coli. Supported by NIH Grant GM030910.