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.
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- Ames G. F., Joshi A. K. Energy coupling in bacterial periplasmic permeases. J Bacteriol. 1990 Aug;172(8):4133–4137. doi: 10.1128/jb.172.8.4133-4137.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Ames G. F., Mimura C. S., Holbrook S. R., Shyamala V. Traffic ATPases: a superfamily of transport proteins operating from Escherichia coli to humans. Adv Enzymol Relat Areas Mol Biol. 1992;65:1–47. doi: 10.1002/9780470123119.ch1. [DOI] [PubMed] [Google Scholar]
- Baichwal V., Liu D., Ames G. F. The ATP-binding component of a prokaryotic traffic ATPase is exposed to the periplasmic (external) surface. Proc Natl Acad Sci U S A. 1993 Jan 15;90(2):620–624. doi: 10.1073/pnas.90.2.620. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Bliss J. M., Garon C. F., Silver R. P. Polysialic acid export in Escherichia coli K1: the role of KpsT, the ATP-binding component of an ABC transporter, in chain translocation. Glycobiology. 1996 Jun;6(4):445–452. doi: 10.1093/glycob/6.4.445. [DOI] [PubMed] [Google Scholar]
- Bliss J. M., Silver R. P. Coating the surface: a model for expression of capsular polysialic acid in Escherichia coli K1. Mol Microbiol. 1996 Jul;21(2):221–231. doi: 10.1046/j.1365-2958.1996.6461357.x. [DOI] [PubMed] [Google Scholar]
- Economou A., Pogliano J. A., Beckwith J., Oliver D. B., Wickner W. SecA membrane cycling at SecYEG is driven by distinct ATP binding and hydrolysis events and is regulated by SecD and SecF. Cell. 1995 Dec 29;83(7):1171–1181. doi: 10.1016/0092-8674(95)90143-4. [DOI] [PubMed] [Google Scholar]
- Economou A., Wickner W. SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion. Cell. 1994 Sep 9;78(5):835–843. doi: 10.1016/s0092-8674(94)90582-7. [DOI] [PubMed] [Google Scholar]
- Higgins C. F. ABC transporters: from microorganisms to man. Annu Rev Cell Biol. 1992;8:67–113. doi: 10.1146/annurev.cb.08.110192.000435. [DOI] [PubMed] [Google Scholar]
- Higgins C. F. The role of ATP in binding-protein-dependent transport systems. Res Microbiol. 1990 Mar-Apr;141(3):353–360. doi: 10.1016/0923-2508(90)90011-e. [DOI] [PubMed] [Google Scholar]
- Kerppola R. E., Ames G. F. Topology of the hydrophobic membrane-bound components of the histidine periplasmic permease. Comparison with other members of the family. J Biol Chem. 1992 Feb 5;267(4):2329–2336. [PubMed] [Google Scholar]
- Kerppola R. E., Shyamala V. K., Klebba P., Ames G. F. The membrane-bound proteins of periplasmic permeases form a complex. Identification of the histidine permease HisQMP complex. J Biol Chem. 1991 May 25;266(15):9857–9865. [PubMed] [Google Scholar]
- Kim Y. J., Rajapandi T., Oliver D. SecA protein is exposed to the periplasmic surface of the E. coli inner membrane in its active state. Cell. 1994 Sep 9;78(5):845–853. doi: 10.1016/s0092-8674(94)90602-5. [DOI] [PubMed] [Google Scholar]
- Mitchell C., Oliver D. Two distinct ATP-binding domains are needed to promote protein export by Escherichia coli SecA ATPase. Mol Microbiol. 1993 Nov;10(3):483–497. doi: 10.1111/j.1365-2958.1993.tb00921.x. [DOI] [PubMed] [Google Scholar]
- Moxon E. R., Kroll J. S. The role of bacterial polysaccharide capsules as virulence factors. Curr Top Microbiol Immunol. 1990;150:65–85. doi: 10.1007/978-3-642-74694-9_4. [DOI] [PubMed] [Google Scholar]
- Pavelka M. S., Jr, Hayes S. F., Silver R. P. Characterization of KpsT, the ATP-binding component of the ABC-transporter involved with the export of capsular polysialic acid in Escherichia coli K1. J Biol Chem. 1994 Aug 5;269(31):20149–20158. [PubMed] [Google Scholar]
- Pavelka M. S., Jr, Wright L. F., Silver R. P. Identification of two genes, kpsM and kpsT, in region 3 of the polysialic acid gene cluster of Escherichia coli K1. J Bacteriol. 1991 Aug;173(15):4603–4610. doi: 10.1128/jb.173.15.4603-4610.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Prossnitz E., Gee A., Ames G. F. Reconstitution of the histidine periplasmic transport system in membrane vesicles. Energy coupling and interaction between the binding protein and the membrane complex. J Biol Chem. 1989 Mar 25;264(9):5006–5014. [PubMed] [Google Scholar]
- Roberts I. S. Bacterial polysaccharides in sickness and in health. The 1995 Fleming Lecture. Microbiology. 1995 Sep;141(Pt 9):2023–2031. doi: 10.1099/13500872-141-9-2023. [DOI] [PubMed] [Google Scholar]
- Schneider E., Hunke S., Tebbe S. The MalK protein of the ATP-binding cassette transporter for maltose of Escherichia coli is accessible to protease digestion from the periplasmic side of the membrane. J Bacteriol. 1995 Sep;177(18):5364–5367. doi: 10.1128/jb.177.18.5364-5367.1995. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Smith A. N., Boulnois G. J., Roberts I. S. Molecular analysis of the Escherichia coli K5 kps locus: identification and characterization of an inner-membrane capsular polysaccharide transport system. Mol Microbiol. 1990 Nov;4(11):1863–1869. doi: 10.1111/j.1365-2958.1990.tb02035.x. [DOI] [PubMed] [Google Scholar]
- Troy F. A., McCloskey M. A. Role of a membranous sialyltransferase complex in the synthesis of surface polymers containing polysialic acid in Escherichia coli. Temperature-induced alteration in the assembly process. J Biol Chem. 1979 Aug 10;254(15):7377–7387. [PubMed] [Google Scholar]
- Vimr E., Steenbergen S., Cieslewicz M. Biosynthesis of the polysialic acid capsule in Escherichia coli K1. J Ind Microbiol. 1995 Oct;15(4):352–360. doi: 10.1007/BF01569991. [DOI] [PubMed] [Google Scholar]
- Walker J. E., Saraste M., Runswick M. J., Gay N. J. Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1982;1(8):945–951. doi: 10.1002/j.1460-2075.1982.tb01276.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Weisgerber C., Troy F. A. Biosynthesis of the polysialic acid capsule in Escherichia coli K1. The endogenous acceptor of polysialic acid is a membrane protein of 20 kDa. J Biol Chem. 1990 Jan 25;265(3):1578–1587. [PubMed] [Google Scholar]