O acetylation of the enterobacterial common antigen polysaccharide is catalyzed by the product of the yiaH gene of Escherichia coli K-12

Junko Kajimura, Arifur Rahman, James Hsu, Matthew R. Evans, Kevin H. Gardner, Paul D. Rick

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

The carbohydrate component of the enterobacterial common antigen (ECA) of Escherichia coli K-12 occurs primarily as a water-soluble cyclic polysaccharide located in the periplasm (ECACYC) and as a phosphoglyceride-linked linear polysaccharide located on the cell surface (ECAPG). The polysaccharides of both forms are comprised of the amino sugars N-acetyl-D-glucosamine (GlcNAc), N-acetyl-D-mannosaminuronic acid (ManNAcA), and 4-acetamido-4,6-dideoxy-D-galactose (Fuc4NAc). These amino sugars are linked to one another to form trisaccharide repeat units with the structure →3-α-D-Fuc4NAc-(1→4)-β-D-ManNAcA-(1→4) -α-D-GlcNAc-(1→. The hydroxyl group in the 6 position of the GlcNAc residues of both ECACYC and ECAPG are nonstoichiometrically esterified with acetyl groups. Random transposon insertion mutagenesis of E. coli K-12 resulted in the generation of a mutant defective in the incorporation of O-acetyl groups into both ECACYC and ECA PG. This defect was found to be due to an insertion of the transposon into the yiaH locus, a putative gene of unknown function located at 80.26 min on the E. coli chromosomal map. Bioinformatic analyses of the predicted yiaH gene product indicate that it is an integral inner membrane protein that is a member of an acyltransferase family of enzymes found in a wide variety of organisms. The results of biochemical and genetic experiments presented here strongly support the conclusion that yiaH encodes the O-acetyltransferase responsible for the incorporation of O-acetyl groups into both ECACYC and ECAPG. Accordingly, we propose that this gene be designated wecH.

Original languageEnglish (US)
Pages (from-to)7542-7550
Number of pages9
JournalJournal of Bacteriology
Volume188
Issue number21
DOIs
StatePublished - Nov 2006

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Acetylation
Amino Sugars
Polysaccharides
Escherichia coli
Glycerophospholipids
Genes
Acyltransferases
Trisaccharides
Periplasm
Acetyltransferases
Acetylglucosamine
Computational Biology
Galactose
Mutagenesis
Hydroxyl Radical
Molecular Biology
Membrane Proteins
Carbohydrates
Water
Enzymes

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Immunology

Cite this

O acetylation of the enterobacterial common antigen polysaccharide is catalyzed by the product of the yiaH gene of Escherichia coli K-12. / Kajimura, Junko; Rahman, Arifur; Hsu, James; Evans, Matthew R.; Gardner, Kevin H.; Rick, Paul D.

In: Journal of Bacteriology, Vol. 188, No. 21, 11.2006, p. 7542-7550.

Research output: Contribution to journalArticle

Kajimura, Junko ; Rahman, Arifur ; Hsu, James ; Evans, Matthew R. ; Gardner, Kevin H. ; Rick, Paul D. / O acetylation of the enterobacterial common antigen polysaccharide is catalyzed by the product of the yiaH gene of Escherichia coli K-12. In: Journal of Bacteriology. 2006 ; Vol. 188, No. 21. pp. 7542-7550.
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abstract = "The carbohydrate component of the enterobacterial common antigen (ECA) of Escherichia coli K-12 occurs primarily as a water-soluble cyclic polysaccharide located in the periplasm (ECACYC) and as a phosphoglyceride-linked linear polysaccharide located on the cell surface (ECAPG). The polysaccharides of both forms are comprised of the amino sugars N-acetyl-D-glucosamine (GlcNAc), N-acetyl-D-mannosaminuronic acid (ManNAcA), and 4-acetamido-4,6-dideoxy-D-galactose (Fuc4NAc). These amino sugars are linked to one another to form trisaccharide repeat units with the structure →3-α-D-Fuc4NAc-(1→4)-β-D-ManNAcA-(1→4) -α-D-GlcNAc-(1→. The hydroxyl group in the 6 position of the GlcNAc residues of both ECACYC and ECAPG are nonstoichiometrically esterified with acetyl groups. Random transposon insertion mutagenesis of E. coli K-12 resulted in the generation of a mutant defective in the incorporation of O-acetyl groups into both ECACYC and ECA PG. This defect was found to be due to an insertion of the transposon into the yiaH locus, a putative gene of unknown function located at 80.26 min on the E. coli chromosomal map. Bioinformatic analyses of the predicted yiaH gene product indicate that it is an integral inner membrane protein that is a member of an acyltransferase family of enzymes found in a wide variety of organisms. The results of biochemical and genetic experiments presented here strongly support the conclusion that yiaH encodes the O-acetyltransferase responsible for the incorporation of O-acetyl groups into both ECACYC and ECAPG. Accordingly, we propose that this gene be designated wecH.",
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