Evidence that KpsT, the ATP-binding component of an ATP-binding cassette transporter, is exposed to the periplasm and associates with polymer during translocation of the polysialic acid capsule of Escherichia coli K1

Author:

Bliss J M1,Silver R P1

Affiliation:

1. Department of Microbiology and Immunology, University of Rochester Medical Center, New York 14642, USA.

Abstract

KpsT utilizes ATP to effect translocation of the polysialic acid capsule of Escherichia coli K1. We have previously proposed a mechanistic model for the action of this protein. Here, we provide evidence to support two predictions of the model: that KpsT associates with polymer and that KpsT is accessible from the periplasmic surface of the inner membrane.

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

Reference25 articles.

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2. Traffic ATPases: a superfamily of transport proteins operating from Escherichia coli to humans;Ames G. F.;Adv. Enzymol.,1992

3. The ATP-binding component of a prokaryotic traffic ATPase is exposed to the periplasmic (external) surface;Baichwal V.;Proc. Natl. Acad. Sci. USA,1993

4. Coating the surface: a model for expression of capsular polysialic acid in Escherichia coli K1;Bliss J. M.;Mol. Microbiol.,1996

5. Polysialic acid export in Escherichia coli K1: the role of KpsT, the ATP-binding component of an ABC transporter, in chain translocation;Bliss J. M.;Glycobiology,1996

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