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The N -Acetylmannosamine Transferase Catalyzes the First Committed Step of Teichoic Acid Assembly in Bacillus subtilis and Staphylococcus aureus
Author(s) -
Michael A. D’Elia,
James A. Henderson,
Terry J. Beveridge,
David E. Heinrichs,
Eric D. Brown
Publication year - 2009
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.00611-08
Subject(s) - teichoic acid , bacillus subtilis , transferase , biology , biochemistry , microbiology and biotechnology , biosynthesis , staphylococcus aureus , glycosyltransferase , gene , enzyme , peptidoglycan , bacteria , genetics
There have been considerable strides made in the characterization of the dispensability of teichoic acid biosynthesis genes in recent years. A notable omission thus far has been an early gene in teichoic acid synthesis encoding the N-acetylmannosamine transferase (tagA in Bacillus subtilis; tarA in Staphylococcus aureus), which adds N-acetylmannosamine to complete the synthesis of undecaprenol pyrophosphate-linked disaccharide. Here, we show that the N-acetylmannosamine transferases are dispensable for growth in vitro, making this biosynthetic enzyme the last dispensable gene in the pathway, suggesting that tagA (or tarA) encodes the first committed step in wall teichoic acid synthesis.

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