Homologous Versus Heterologous Interactions in the Bicomponent Staphylococcal Gamma-haemolysin Pore

Overview

Journal Biochem J

Specialty Biochemistry

Date 2005 Oct 26

PMID 16241903

Citations 5

Authors

Gabriella Viero

Romina Cunaccia

Gilles Prevost

Sandra Werner

Henri Monteil

Daniel Keller

Olivier Joubert

Gianfranco Menestrina

Mauro Dalla Serra

Affiliations

Soon will be listed here.

Abstract

Staphylococcal gamma-haemolysin HlgA-HlgB forms a beta-barrel transmembrane pore in cells and in model membranes. The pore is formed by the oligomerization of two different proteins and a still debated number of monomers. To clarify the topology of the pore, we have mutated single residues - placed near the right and left interfaces of each monomer into cysteine. The mutants were labelled with fluorescent probes, forming a donor-acceptor pair for FRET (fluorescence resonance energy transfer). Heterologous couples (labelled on complementary left and right interfaces) displayed a marked FRET, suggesting extensive HlgA-HlgB or HlgB-HlgA contacts. Heterologous control couples (with both components labelled on the same side) showed absent or low FRET. We found the same result for the homologous couple formed by HlgA [i.e. HlgA-HlgA in the presence of wt (wild-type) HlgB]. The homologous HlgB couple (HlgB-HlgB labelled on left and right interfaces and in the presence of wt HlgA) displayed a transient, declining FRET, which may indicate fast formation of an intermediate that is consumed during pore formation. We conclude that bicomponent pores are assembled by alternating heterologous monomers.

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