Folding and aggregation of export-defective mutants of the maltose-binding protein

被引:8
作者
Betton, JM [1 ]
Phichith, D [1 ]
Hunke, S [1 ]
机构
[1] Inst Pasteur, CNRS URA 2185, Unite Repliement & Modelisat Prot, F-75724 Paris 15, France
关键词
heat-shock proteins; maltose; protein folding; protein precursors;
D O I
10.1016/S0923-2508(02)01338-4
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
We previously characterized a defective-folding variant of the periplasmic maltose-binding protein, MalE31. To examine the alternative folding pathways open to the MalE31 precursor, we have analyzed the cellular fates of this aggregation-prone protein carrying altered signal sequences. Our results are most easily interpreted by a kinetic competition between exportation, folding, and degradation. (C) 2002 Editions scientifiques et medicales Elsevier SAS. All rights reserved.
引用
收藏
页码:399 / 404
页数:6
相关论文
共 25 条
[1]  
[Anonymous], 1996, ESCHERICHIA COLI SAL
[2]   EXPORT OF THE PERIPLASMIC MALTOSE-BINDING PROTEIN OF ESCHERICHIA-COLI [J].
BASSFORD, PJ .
JOURNAL OF BIOENERGETICS AND BIOMEMBRANES, 1990, 22 (03) :401-439
[3]   MUTATIONS WHICH ALTER THE FUNCTION OF THE SIGNAL SEQUENCE OF THE MALTOSE BINDING-PROTEIN OF ESCHERICHIA-COLI [J].
BEDOUELLE, H ;
BASSFORD, PJ ;
FOWLER, AV ;
ZABIN, I ;
BECKWITH, J ;
HOFNUNG, M .
NATURE, 1980, 285 (5760) :78-81
[4]   IN-VIVO ASSEMBLY OF ACTIVE MALTOSE-BINDING PROTEIN FROM INDEPENDENTLY EXPORTED PROTEIN-FRAGMENTS [J].
BETTON, JM ;
HOFNUNG, M .
EMBO JOURNAL, 1994, 13 (05) :1226-1234
[5]   Folding of a mutant maltose-binding protein of Escherichia coli which forms inclusion bodies [J].
Betton, JM ;
Hofnung, M .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (14) :8046-8052
[6]   Probing the structural role of an alpha beta loop of maltose-binding protein by mutagenesis: Heat-shock induction by loop variants of the maltose-binding protein that form periplasmic inclusion bodies [J].
Betton, JM ;
Boscus, D ;
Missiakas, D ;
Raina, S ;
Hofnung, M .
JOURNAL OF MOLECULAR BIOLOGY, 1996, 262 (02) :140-150
[7]   Degradation versus aggregation of misfolded maltose-binding protein in the periplasm of Escherichia coli [J].
Betton, JM ;
Sassoon, N ;
Hofnung, M ;
Laurent, M .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (15) :8897-8902
[8]   A newly synthesized, ribosome-bound polypeptide chain adopts conformations dissimilar from early in vitro refolding intermediates [J].
Clark, PL ;
King, J .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (27) :25411-25420
[9]   Targeting and assembly of periplasmic and outer-membrane proteins in Escherichia coli [J].
Danese, PN ;
Silhavy, TJ .
ANNUAL REVIEW OF GENETICS, 1998, 32 :59-94
[10]   The structural basis of protein targeting and translocation in bacteria [J].
Driessen, AJM ;
Manting, EH ;
van der Does, C .
NATURE STRUCTURAL BIOLOGY, 2001, 8 (06) :492-498