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J Biol Chem, Vol. 274, Issue 49, 35129-35138, December 3, 1999
From the During O antigen lipopolysaccharide (LPS)
synthesis in bacteria, transmembrane migration of
undecaprenylpyrophosphate (Und-P-P)-bound O antigen subunits occurs
before their polymerization and ligation to the rest of the LPS
molecule. Despite the general nature of the translocation process,
putative O-antigen translocases display a low level of amino acid
sequence similarity. In this work, we investigated whether complete O
antigen subunits are required for translocation. We demonstrate that a
single sugar, GlcNAc, can be incorporated to LPS of Escherichia
coli K-12. This incorporation required the functions of two O
antigen synthesis genes, wecA (UDP-GlcNAc:Und-P GlcNAc-1-P
transferase) and wzx (O-antigen translocase). Complementation experiments with putative O-antigen translocases from
E. coli O7 and Salmonella enterica indicated
that translocation of O antigen subunits is independent of the chemical
structure of the saccharide moiety. Furthermore, complementation with
putative translocases involved in synthesis of exopolysaccharides
demonstrated that these proteins could not participate in O antigen
assembly. Our data indicate that recognition of a complete
Und-P-P-bound O antigen subunit is not required for translocation and
suggest a model for O antigen synthesis involving recognition of
Und-P-P-linked sugars by a putative complex made of Wzx translocase and
other proteins involved in the processing of O antigen.
The Activity of a Putative Polyisoprenol-linked Sugar Translocase
(Wzx) Involved in Escherichia coli O Antigen Assembly Is
Independent of the Chemical Structure of the O Repeat
,
,,, and Instituto de Investigaciones
Bioquímicas Fundación Campomar, Buenos Aires, Argentina,
the ¶ Department of Microbiology and Immunology, University of
Western Ontario, London, Ontario N6A 5C1, Canada, and the
Institute for Biological Sciences, National Research Council,
Ottawa, Ontario K1A 0R6, Canada
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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