Science. 1990 May 18;248(4957):860-3.

No specific recognition of leader peptide by SecB, a chaperone involved in protein export.

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Biochemistry/Biophysics Program, Washington State University, Pullman 99164-4660.

Abstract

Most proteins destined for export from Escherichia coli are made as precursors containing amino-terminal leader sequences that are essential for export and that are removed during the process. The initial step in export of a subset of proteins, which includes maltose-binding protein, is binding of the precursor by the molecular chaperone SecB. This work shows directly that SecB binds with high affinity to unfolded maltose-binding protein but does not specifically recognize and bind the leader. Rather, the leader modulates folding to expose elements in the remainder of the polypeptide that are recognized by SecB.

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Physiological role during export for the retardation of folding by the leader peptide of maltose-binding protein. [Proc Natl Acad Sci U S A. 1989]
Physiological role during export for the retardation of folding by the leader peptide of maltose-binding protein.
Liu G, Topping TB, Randall LL. Proc Natl Acad Sci U S A. 1989 Dec; 86(23):9213-7.
High-affinity binding of Escherichia coli SecB to the signal sequence region of a presecretory protein. [Proc Natl Acad Sci U S A. 1995]
High-affinity binding of Escherichia coli SecB to the signal sequence region of a presecretory protein.
Watanabe M, Blobel G. Proc Natl Acad Sci U S A. 1995 Oct 24; 92(22):10133-6.
SecB-independent export of Escherichia coli ribose-binding protein (RBP): some comparisons with export of maltose-binding protein (MBP) and studies with RBP-MBP hybrid proteins. [J Bacteriol. 1990]
SecB-independent export of Escherichia coli ribose-binding protein (RBP): some comparisons with export of maltose-binding protein (MBP) and studies with RBP-MBP hybrid proteins.
Collier DN, Strobel SM, Bassford PJ Jr. J Bacteriol. 1990 Dec; 172(12):6875-84.
Review Export of the periplasmic maltose-binding protein of Escherichia coli. [J Bioenerg Biomembr. 1990]
Review Export of the periplasmic maltose-binding protein of Escherichia coli.
Bassford PJ Jr. J Bioenerg Biomembr. 1990 Jun; 22(3):401-39.
Review Recognition of ligands by SecB, a molecular chaperone involved in bacterial protein export. [Philos Trans R Soc Lond B Biol...]
Review Recognition of ligands by SecB, a molecular chaperone involved in bacterial protein export.
Hardy SJ, Randall LL. Philos Trans R Soc Lond B Biol Sci. 1993 Mar 29; 339(1289):343-52; discussion 352-4.

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Cited by 37 PubMed Central articles

Preparation of a highly translocation-competent proOmpA/SecB complex. [Protein Sci. 2010]
Preparation of a highly translocation-competent proOmpA/SecB complex.
Nishiyama K, Tokuda H. Protein Sci. 2010 Dec; 19(12):2402-8.
SecB is a bona fide generalized chaperone in Escherichia coli. [Proc Natl Acad Sci U S A. 2004]
SecB is a bona fide generalized chaperone in Escherichia coli.
Ullers RS, Luirink J, Harms N, Schwager F, Georgopoulos C, Genevaux P. Proc Natl Acad Sci U S A. 2004 May 18; 101(20):7583-8. Epub 2004 May 5.
Recognition of secretory proteins in Escherichia coli requires signals in addition to the signal sequence and slow folding. [BMC Microbiol. 2002]
Recognition of secretory proteins in Escherichia coli requires signals in addition to the signal sequence and slow folding.
Mallik I, Smith MA, Flower AM. BMC Microbiol. 2002 Nov 11; 2:32. Epub 2002 Nov 11.

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No specific recognition of leader peptide by SecB, a chaperone involved in protein export.

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