Folding and aggregation of export-defective mutants of the maltose-binding protein
被引:8
作者:
Betton, JM
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机构:
Inst Pasteur, CNRS URA 2185, Unite Repliement & Modelisat Prot, F-75724 Paris 15, FranceInst Pasteur, CNRS URA 2185, Unite Repliement & Modelisat Prot, F-75724 Paris 15, France
Betton, JM
[1
]
Phichith, D
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机构:
Inst Pasteur, CNRS URA 2185, Unite Repliement & Modelisat Prot, F-75724 Paris 15, FranceInst Pasteur, CNRS URA 2185, Unite Repliement & Modelisat Prot, F-75724 Paris 15, France
Phichith, D
[1
]
Hunke, S
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h-index: 0
机构:
Inst Pasteur, CNRS URA 2185, Unite Repliement & Modelisat Prot, F-75724 Paris 15, FranceInst Pasteur, CNRS URA 2185, Unite Repliement & Modelisat Prot, F-75724 Paris 15, France
Hunke, S
[1
]
机构:
[1] Inst Pasteur, CNRS URA 2185, Unite Repliement & Modelisat Prot, F-75724 Paris 15, France
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.