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J. Biol. Chem., Vol. 276, Issue 4, 2361-2371, January 26, 2001
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From the Department of Microbiology, University of Guelph, Guelph,
Ontario, N1G 2W1 Canada
Wzc proteins are tyrosine autokinases. They are
found in some important bacterial pathogens of humans and livestock as
well as plant-associated bacteria, and are often encoded within gene clusters determining synthesis and assembly of capsular and
extracellular polysaccharides. Autophosphorylation of
Wzccps is essential for assembly of the serotype K30
group 1 capsule in Escherichia coli O9a:K30, although a
genetically unlinked Wzccps-homologue (Etk) can also
participate with low efficiency. While autophosphorylation of
Wzccps is required for assembly of high molecular weight
K30 capsular polysaccharide, it is not essential for either the
synthesis of the K30 repeat units or for activity of the K30 polymerase enzyme. Paradoxically, the cognate phosphotyrosine protein phosphatase for Wzccps, Wzbcps, is also required for
capsule expression. The tyrosine-rich domain at the C terminus of
Wzccps was identified as the site of phosphorylation and
autophosphorylation of Wzc requires a functional Walker A motif.
Intermolecular transphosphorylation of Wzccps was detected
in strains expressing a combination of mutant Wzccps
derivatives. The N- and C-terminal domains of Wzccps were
expressed independently to mimic the situation found naturally in
Gram-positive bacteria. In this format, both domains were required for
phosphorylation of the Wzccps C terminus, and for capsule assembly. Regulation by a post-translational phosphorylation event represents a new dimension in the assembly of bacterial cell-surface polysaccharides.
Phosphorylation of Wzc, a Tyrosine Autokinase, Is Essential for
Assembly of Group 1 Capsular Polysaccharides in Escherichia
coli*
,
*
This work was supported in part by an operating grant from
the Canadian Institutes of Health Research (to C. W.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Supported by Erwin Schrödinger Postdoctoral Fellowship
J1594-GEN from the Austrian Science Fund.
§
Supported by postgraduate scholarships from the Natural Science and
Engineering Research Council of Canada.
¶
Received an undergraduate (USRA) award from the Natural
Science and Engineering Research Council of Canada.
Canadian Institutes of Health Research Senior Scientist. To
whom correspondence should be addressed: Dept. of Microbiology, University of Guelph, Guelph, Ontario, N1G 2W1 Canada. Tel.:
519-824-4120 (ext. 3478); Fax: 519-837-1802; E-mail:
cwhitfie@uoguelph.ca.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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