Escherichia coli ClpB is a non-processive polypeptide translocase

Autor: Aaron L. Lucius, JiaBei Lin, Clarissa L. Weaver, Tao Li, Elizabeth C. Duran, Justin M. Miller

Publikováno v: Biochemical Journal

Here we show that ClpB is a non-processive translocase that takes, at most, two steps on the polypeptide backbone before dissociation. These findings indicate that ClpB is not likely to translocate polypeptide through its axial channel as previously

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http://europepmc.org/articles/PMC4692069

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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.

Publikováno v: The Biochemical journal [Biochem J] 2015 Aug 15; Vol. 470 (1), pp. 39-52. Date of Electronic Publication: 2015 Jun 11.

E. coli ClpA catalyzed polypeptide translocation is allosterically controlled by the protease ClpP.

Autor: Miller JM; Department of Chemistry, The University of Alabama at Birmingham, 1530 Third Avenue South, Birmingham, AL 35294-1240, USA., Lin J, Li T, Lucius AL

Publikováno v: Journal of molecular biology [J Mol Biol] 2013 Aug 09; Vol. 425 (15), pp. 2795-812. Date of Electronic Publication: 2013 Apr 29.