Neisseria gonorrhoeae porin, P.IB, causes release of ATP from yeast actin

Kuo-Kuang Wen; Milan S Blake; Peter A Rubenstein

doi:10.1007/s10974-004-6069-y

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Neisseria gonorrhoeae porin, P.IB, causes release of ATP from yeast actin

Journal article

Peer reviewed

Neisseria gonorrhoeae porin, P.IB, causes release of ATP from yeast actin

Kuo-Kuang Wen, Milan S Blake and Peter A Rubenstein

Journal of muscle research and cell motility, Vol.25(4-5), pp.343-350

2004

DOI: 10.1007/s10974-004-6069-y

PMID: 15548863

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Abstract

Neisserial porins may play a role in the invasion of the host cell by the bacterium. The protein translocates to the host cell membrane and then to the cytosol during the invasive process, and we have shown it interacts with actin in vitro. Here, we have examined the nucleotide-dependence of the interaction of Neisseria porin, P.IB, with fluorescently labeled yeast G actin. Increasing free ATP between 0 to 0.5 mM retards complex formation between the two proteins. The ATP effect probably results from binding of the nucleotide to actin rather than to porin. Complex formation results in a biphasic release of bound nucleoside triphosphate from actin in the absence of free nucleotide at a rate slower than that of complex formation, but it does not induce hydrolysis of the actin-bound nucleotide. ATP prevents the porin-induced distortion of F-actin structure, and addition of ATP to the complex formed in the absence of free nucleotide induces actin polymerization indicating that P.IB stabilizes nucleotide-free G-actin. Our results suggest that P.IB causes an actin conformation change leading to the production of a polymerization-competent nucleotide-free protein.

Fluorescent Dyes - chemistry

Microscopy, Electron, Transmission

Bacterial Adhesion - physiology

Adenosine Triphosphate - metabolism

Actins - metabolism

Porins - metabolism

Bacterial Adhesion - genetics

Mutation - genetics

Neisseria gonorrhoeae - metabolism

Protein Transport

Yeasts - metabolism

Details

Title: Subtitle: Neisseria gonorrhoeae porin, P.IB, causes release of ATP from yeast actin
Creators: Kuo-Kuang Wen - Department of Biochemistry, University of Iowa Carver College of Medicine, Iowa City, IA 52242, USA
Milan S Blake
Peter A Rubenstein
Resource Type: Journal article
Publication Details: Journal of muscle research and cell motility, Vol.25(4-5), pp.343-350
Publisher: Netherlands
DOI: 10.1007/s10974-004-6069-y
PMID: 15548863
ISSN: 0142-4319
eISSN: 1573-2657
Grant note: AI45728 / NIAID NIH HHS
Language: English
Date published: 2004
Academic Unit: Stead Family Department of Pediatrics; Biochemistry and Molecular Biology; Internal Medicine
Record Identifier: 9984024515702771

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