Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 356, Issue 3, Pages 604-609Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2007.03.015
Keywords
O-antigen; UDP-hexose 4-epimerase; rough LPS; semi-rough LPS
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The O-antigen gene cluster of Escherichia coli 086:137 was sequenced previously in our lab. One UDP-hexose 4-epimerase gene (named gne2 in this paper) was found and later characterized to be able to catalyze the interconversion between UDP-GlcNAc/GalNAc and UDP-Glc/Gal with almost equal efficiency. However, sequencing of the flanking gene region upstream of the traditional O-antigen gene cluster revealed an open reading frame (griel), sharing 100% identity with Gne from E coli 055, previously identified as UDP-GlcNAc 4-epimerase. Furthermore, we also located the traditional galE gene in the gal operon of O86:B7, which can catalyze the interconversion of UDP-Glc to UDP-Gal. Thus, for the first time, three UDP-hexose 4-epimerases with overlapping substrate specificity were found to coexist in one bacterium. Deletion of gne1 and gne2 in 086:137 produced two different LPS phenotypes: the gne1 mutant exhibited rough LPS, while the gne2 mutant showed semi-rough LPS phenotype. These findings provide new clues for understanding the mechanism of O-antigen biosynthesis. (c) 2007 Elsevier Inc. All rights reserved.
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