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Science 25 January 1991:
Vol. 251. no. 4992, pp. 439 - 443
DOI: 10.1126/science.1989077
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Articles

Science, Vol 251, Issue 4992, 439-443
Copyright © 1991 by American Association for the Advancement of Science

articles

A kinetic partitioning model of selective binding of nonnative proteins by the bacterial chaperone SecB

SJ Hardy and LL Randall

Department of Biochemistry and Biophysics, Washington State University, Pullman 99164-4660.

An in vitro assay for the interaction of SecB, a molecular chaperone from Escherichia coli, with polypeptide ligands was established based on the ability of SecB to block the refolding of denatured maltose-binding protein. Competition experiments show that SecB binds selectively to nonnative proteins with high affinity and without specificity for a particular sequence of amino acids. It is proposed that selectivity in binding is due to a kinetic partitioning of polypeptides between folding and association with SecB.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Direct Observation of Chaperone-Induced Changes in a Protein Folding Pathway.
P. Bechtluft, R. G. H. van Leeuwen, M. Tyreman, D. Tomkiewicz, N. Nouwen, H. L. Tepper, A. J. M. Driessen, and S. J. Tans (2007)
Science 318, 1458-1461
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From the Cover: A selection for mutants that interfere with folding of Escherichia coli thioredoxin-1 in vivo.
D. Huber, M.-i. Cha, L. Debarbieux, A.-G. Planson, N. Cruz, G. Lopez, M. L. Tasayco, A. Chaffotte, and J. Beckwith (2005)
PNAS 102, 18872-18877
   Abstract »    Full Text »    PDF »
Use of Thioredoxin as a Reporter To Identify a Subset of Escherichia coli Signal Sequences That Promote Signal Recognition Particle-Dependent Translocation.
D. Huber, D. Boyd, Y. Xia, M. H. Olma, M. Gerstein, and J. Beckwith (2005)
J. Bacteriol. 187, 2983-2991
   Abstract »    Full Text »    PDF »
SecB is a bona fide generalized chaperone in Escherichia coli.
R. S. Ullers, J. Luirink, N. Harms, F. Schwager, C. Georgopoulos, and P. Genevaux (2004)
PNAS 101, 7583-7588
   Abstract »    Full Text »    PDF »
Antifolding Activity of the SecB Chaperone Is Essential for Secretion of HasA, a Quickly Folding ABC Pathway Substrate.
N. Wolff, G. Sapriel, C. Bodenreider, A. Chaffotte, and P. Delepelaire (2003)
J. Biol. Chem. 278, 38247-38253
   Abstract »    Full Text »    PDF »
Genetic Analysis of Pathway Specificity during Posttranslational Protein Translocation across the Escherichia coli Plasma Membrane.
N. Blaudeck, P. Kreutzenbeck, R. Freudl, and G. A. Sprenger (2003)
J. Bacteriol. 185, 2811-2819
   Abstract »    Full Text »    PDF »
DnaK Promotes the Selective Export of Outer Membrane Protein Precursors in SecA-deficient Escherichia coli.
H.-Y. Qi, J. B. Hyndman, and H. D. Bernstein (2002)
J. Biol. Chem. 277, 51077-51083
   Abstract »    Full Text »    PDF »
Trigger Factor Retards Protein Export in Escherichia coli.
H. C. Lee and H. D. Bernstein (2002)
J. Biol. Chem. 277, 43527-43535
   Abstract »    Full Text »    PDF »
SecB Dependence of an Exported Protein Is a Continuum Influenced by the Characteristics of the Signal Peptide or Early Mature Region.
J. Kim, J. Luirink, and D. A. Kendall (2000)
J. Bacteriol. 182, 4108-4112
   Abstract »    Full Text »
A Thermodynamic Coupling Mechanism for the Disaggregation of a Model Peptide Substrate by Chaperone SecB.
V. G. Panse, P. Vogel, W. E. Trommer, and R. Varadarajan (2000)
J. Biol. Chem. 275, 18698-18703
   Abstract »    Full Text »    PDF »
Substrate Specificity of the SecB Chaperone.
N. T. M. Knoblauch, S. Rudiger, H.-J. Schonfeld, A. J. M. Driessen, J. Schneider-Mergener, and B. Bukau (1999)
J. Biol. Chem. 274, 34219-34225
   Abstract »    Full Text »    PDF »
Yersinia enterocolitica Type III Secretion. ON THE ROLE OF SycE IN TARGETING YopE INTO HeLa CELLS.
L. W. Cheng and O. Schneewind (1999)
J. Biol. Chem. 274, 22102-22108
   Abstract »    Full Text »    PDF »
Mutational Alterations in the Homotetrameric Chaperone SecB That Implicate the Structure as Dimer of Dimers.
E. M. Muren, D. Suciu, T. B. Topping, C. A. Kumamoto, and L. L. Randall (1999)
J. Biol. Chem. 274, 19397-19402
   Abstract »    Full Text »    PDF »
Protein Targeting to the Bacterial Cytoplasmic Membrane.
P. Fekkes and A. J. M. Driessen (1999)
Microbiol. Mol. Biol. Rev. 63, 161-173
   Abstract »    Full Text »    PDF »
Endogenous SecA Catalyzes Preprotein Translocation at SecYEG.
J. Eichler, K. Rinard, and W. Wickner (1998)
J. Biol. Chem. 273, 21675-21681
   Abstract »    Full Text »    PDF »
Cotranslational Protein Folding.
A. N. Fedorov and T. O. Baldwin (1997)
J. Biol. Chem. 272, 32715-32718
   Full Text »    PDF »
Kinetic Partitioning. POISING SecB TO FAVOR ASSOCIATION WITH A RAPIDLY FOLDING LIGAND.
D. L. Diamond and L. L. Randall (1997)
J. Biol. Chem. 272, 28994-28998
   Abstract »    Full Text »    PDF »
Chaperone SecB from Escherichia coli Mediates Kinetic Partitioning via a Dynamic Equilibrium with Its Ligands.
T. B. Topping and L. L. Randall (1997)
J. Biol. Chem. 272, 19314-19318
   Abstract »    Full Text »    PDF »
Refolding Intermediates of Acid-unfolded Mitochondrial Aspartate Aminotransferase Bind to hsp70.
A. Artigues, A. Iriarte, and M. Martinez-Carrion (1997)
J. Biol. Chem. 272, 16852-16861
   Abstract »    Full Text »    PDF »
Binding of SecB to ribosome-bound polypeptides has the same characteristics as binding to full-length, denatured proteins.
L. L. Randall, T. B. Topping, S. J. S. Hardy, M. Y. Pavlov, D. V. Freistroffer, and M. Ehrenberg (1997)
PNAS 94, 802-807
   Abstract »    Full Text »    PDF »
Escherichia coli Preprotein Translocase.
W. Wickner and M. R. Leonard (1996)
J. Biol. Chem. 271, 29514-29516
   Full Text »    PDF »
Diverse Effects of Mutation on the Activity of the Escherichia coli Export Chaperone SecB.
H. H. Kimsey, M. D. Dagarag, and C. A. Kumamoto (1995)
J. Biol. Chem. 270, 22831-22835
   Abstract »    Full Text »    PDF »
Exposure of Hydrophobic Surfaces on the Chaperonin GroEL Oligomer by Protonation or Modification of His-401.
D. L. Gibbons and D. L. Gibbons (1995)
J. Biol. Chem. 270, 7335-7340
   Abstract »    Full Text »    PDF »
Peptide binding by chaperone SecB: implications for recognition of nonnative structure.
L. Randall (1992)
Science 257, 241-245
   Abstract »    PDF »
DnaK and DnaJ heat shock proteins participate in protein export in Escherichia coli..
J Wild, E Altman, T Yura, and C A Gross (1992)
Genes & Dev. 6, 1165-1172
   Abstract »    PDF »
Electron Spin Resonance and Fluorescence Studies of the Bound-state Conformation of a Model Protein Substrate to the Chaperone SecB.
V. G. Panse, K. Beena, R. Philipp, W. E. Trommer, P. D. Vogel, and R. Varadarajan (2001)
J. Biol. Chem. 276, 33681-33688
   Abstract »    Full Text »    PDF »
Indecisive M13 Procoat Protein Mutants Bind to SecA but Do Not Activate the Translocation ATPase.
T. Roos, D. Kiefer, S. Hugenschmidt, A. Economou, and A. Kuhn (2001)
J. Biol. Chem. 276, 37909-37915
   Abstract »    Full Text »    PDF »


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