The HtrA family of proteases: Implications for protein composition and cell fate

被引：545

作者：

Clausen, T

Southan, C

Ehrmann, M

机构：

[1] Max Planck Inst Biochem, D-82152 Martinsried, Germany

[2] Cardiff Univ, Sch Biosci, Cardiff CF10 3US, S Glam, Wales

[3] Oxford GlycoSci UK Ltd, Abingdon OX14 4RY, Oxon, England

来源：

MOLECULAR CELL | 2002年 / 10卷 / 03期

基金：

英国生物技术与生命科学研究理事会;

关键词：

D O I：

10.1016/S1097-2765(02)00658-5

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：

Cells precisely monitor the concentration and functionality of each protein for optimal performance. Protein quality control involves molecular chaperones, folding catalysts, and proteases that are often heat shock proteins. One quality control factor is HtrA, one of a new class of oligomeric serine proteases. The defining feature of the HtrA family is the combination of a catalytic domain with at least one C-terminal PDZ domain. Here, we discuss the properties and roles of this ATP-independent protease chaperone system in protein metabolism and cell fate.

引用

收藏

页码：443 / 455

页数：13

相关论文

共 69 条

[1] degS (hhoB) is an essential Escherichia coli gene whose indispensable function is to provide σE activity [J].

Alba, BM ;

Zhong, HJ ;

Pelayo, JC ;

Gross, CA .

MOLECULAR MICROBIOLOGY, 2001, 40 (06) :1323-1333

[2] The InterPro database, an integrated documentation resource for protein families, domains and functional sites [J].

Apweiler, R ;

Attwood, TK ;

Bairoch, A ;

Bateman, A ;

Birney, E ;

Biswas, M ;

Bucher, P ;

Cerutti, T ;

Corpet, F ;

Croning, MDR ;

Durbin, R ;

Falquet, L ;

Fleischmann, W ;

Gouzy, J ;

Hermjakob, H ;

Hulo, N ;

Jonassen, I ;

Kahn, D ;

Kanapin, A ;

Karavidopoulou, Y ;

Lopez, R ;

Marx, B ;

Mulder, NJ ;

Oinn, TM ;

Pagni, M ;

Servant, F ;

Sigrist, CJA ;

Zdobnov, EM .

NUCLEIC ACIDS RESEARCH, 2001, 29 (01) :37-40

[3] Overproduction of the Bradyrhizobium japonicum c-type cytochrome subunits of the cbb3 oxidase in Escherichia coli [J].

Arslan, E ;

Schulz, H ;

Zufferey, R ;

Künzler, P ;

Thöny-Meyer, L .

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1998, 251 (03) :744-747

[4]

BALDI A, 2002, IN PRESS ONCOGENE

[5] CONSTRUCTION AND CHARACTERIZATION OF ESCHERICHIA-COLI STRAINS DEFICIENT IN MULTIPLE SECRETED PROTEASES - PROTEASE-III DEGRADES HIGH-MOLECULAR-WEIGHT SUBSTRATES INVIVO [J].

BANEYX, F ;

GEORGIOU, G .

JOURNAL OF BACTERIOLOGY, 1991, 173 (08) :2696-2703

[6] Multicopy suppressors of prc mutant Escherichia coli include two HtrA (DegP) protease homologs (HhoAB), DksA, and a truncated RlpA [J].

Bass, S ;

Gu, QM ;

Christen, A .

JOURNAL OF BACTERIOLOGY, 1996, 178 (04) :1154-1161

[7]

Beeley L J, 2000, Prog Med Chem, V37, P1, DOI 10.1016/S0079-6468(08)70056-0

[8] 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

[9] The structures of HsIU and ATP-dependent protease HsIU-HsIV [J].

Bochtler, M ;

Hartmann, C ;

Song, HK ;

Bourenkov, GP ;

Bartunik, HD ;

Huber, R .

NATURE, 2000, 403 (6771) :800-805

[10] Crystal structure of heat shock locus V (HslV) from Escherichia coli [J].

Bochtler, M ;

Ditzel, L ;

Groll, M ;

Huber, R .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (12) :6070-6074

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