PDZ domains determine the native oligomeric structure of the DegP (HtrA) protease

被引:37
作者
Sassoon, N [1 ]
Arié, JP [1 ]
Betton, JM [1 ]
机构
[1] Inst Pasteur, Unite Programmat Mol & Toxicol Genet, CNRS URA1444, Dept Biotechnol, F-75015 Paris, France
关键词
D O I
10.1046/j.1365-2958.1999.01505.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
DegP (HtrA) is a periplasmic heat shock serine protease of Escherichia coli that degrades misfolded proteins at high temperatures. Biochemical and biophysical experiments have indicated that the purified DegP exists as a hexamer. To examine whether the PDZ domains of DegP were required for oligomerization, we constructed a DegP variant lacking both PDZ domains. This truncated variant, DegP Delta, exhibited no proteolytic activity but exerted a dominant-negative effect on growth at high temperatures by interfering with the functional assembly of oligomeric DegP. Thus, the PDZ domains contain information necessary for proper assembly of the functional hexameric structure of DegP.
引用
收藏
页码:583 / 589
页数:7
相关论文
共 27 条
[1]   The proteasome:: Paradigm of a self-compartmentalizing protease [J].
Baumeister, W ;
Walz, J ;
Zühl, F ;
Seemuller, E .
CELL, 1998, 92 (03) :367-380
[2]   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
[3]   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
[4]   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
[5]   THE CPX 2-COMPONENT SIGNAL-TRANSDUCTION PATHWAY OF ESCHERICHIA-COLI REGULATES TRANSCRIPTION OF THE GENE SPECIFYING THE STRESS-INDUCIBLE PERIPLASMIC PROTEASE, DEGP [J].
DANESE, PN ;
SNYDER, WB ;
COSMA, CL ;
DAVIS, LJB ;
SILHAVY, TJ .
GENES & DEVELOPMENT, 1995, 9 (04) :387-398
[6]   Crystal structure of the hCASK PDZ domain reveals the structural basis of class II PDZ domain target recognition [J].
Daniels, DL ;
Cohen, AR ;
Anderson, JM ;
Brünger, AT .
NATURE STRUCTURAL BIOLOGY, 1998, 5 (04) :317-325
[7]   The permeability of the wall fabric of Escherichia coli and Bacillus subtilis [J].
Demchick, P ;
Koch, AL .
JOURNAL OF BACTERIOLOGY, 1996, 178 (03) :768-773
[8]   Crystal structures of a complexed and peptide-free membrane protein-binding domain: Molecular basis of peptide recognition by PDZ [J].
Doyle, DA ;
Lee, A ;
Lewis, J ;
Kim, E ;
Sheng, M ;
MacKinnon, R .
CELL, 1996, 85 (07) :1067-1076
[9]   Protein quality control: Triage by chaperones and proteases [J].
Gottesman, S ;
Wickner, S ;
Maurizi, MR .
GENES & DEVELOPMENT, 1997, 11 (07) :815-823
[10]   Defective export in Escherichia coli caused by DsbA'-PhoA hybrid proteins whose DsbA' domain cannot fold into a conformation resistant to periplasmic proteases [J].
Guigueno, A ;
Belin, P ;
Boquet, PL .
JOURNAL OF BACTERIOLOGY, 1997, 179 (10) :3260-3269