Escherichia coli ClpB is a non-processive polypeptide translocase.

Autor:	Li T; Department of Chemistry, The University of Alabama at Birmingham (UAB), Birmingham AL, U.S.A., Weaver CL; Department of Chemistry, The University of Alabama at Birmingham (UAB), Birmingham AL, U.S.A., Lin J; Department of Chemistry, The University of Alabama at Birmingham (UAB), Birmingham AL, U.S.A., Duran EC; Department of Chemistry, The University of Alabama at Birmingham (UAB), Birmingham AL, U.S.A., Miller JM; Department of Chemistry, The University of Alabama at Birmingham (UAB), Birmingham AL, U.S.A., Lucius AL; Department of Chemistry, The University of Alabama at Birmingham (UAB), Birmingham AL, U.S.A. allucius@uab.edu.
Jazyk:	angličtina
Zdroj:	The Biochemical journal [Biochem J] 2015 Aug 15; Vol. 470 (1), pp. 39-52. Date of Electronic Publication: 2015 Jun 11.
DOI:	10.1042/BJ20141457
Abstrakt:	Escherichia coli caseinolytic protease (Clp)B is a hexameric AAA+ [expanded superfamily of AAA (ATPase associated with various cellular activities)] enzyme that has the unique ability to catalyse protein disaggregation. Such enzymes are essential for proteome maintenance. Based on structural comparisons to homologous enzymes involved in ATP-dependent proteolysis and clever protein engineering strategies, it has been reported that ClpB translocates polypeptide through its axial channel. Using single-turnover fluorescence and anisotropy experiments we show that ClpB is a non-processive polypeptide translocase that catalyses disaggregation by taking one or two translocation steps followed by rapid dissociation. Using single-turnover FRET experiments we show that ClpB containing the IGL loop from ClpA does not translocate substrate through its axial channel and into ClpP for proteolytic degradation. Rather, ClpB containing the IGL loop dysregulates ClpP leading to non-specific proteolysis reminiscent of ADEP (acyldepsipeptide) dysregulation. Our results support a molecular mechanism where ClpB catalyses protein disaggregation by tugging and releasing exposed tails or loops. (© 2015 Authors; published by Portland Press Limited.)
Databáze:	MEDLINE
Externí odkaz:	Zobrazit plný text záznamu