Hsc62, a new DnaK homologue of Escherichia coli

被引：23

作者：

Yoshimune, K ^{[1
]}

Yoshimura, T ^{[1
]}

Esaki, N ^{[1
]}

机构：

[1] Kyoto Univ, Inst Chem Res, Uji, Kyoto 611, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1998年 / 250卷 / 01期

关键词：

D O I：

10.1006/bbrc.1998.9255

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：

We have cloned and expressed the ORF o170#1 of Escherichia coli, which encodes a 62-kDa protein sharing 33% homology in primary structure with DnaK and Hsc66, Hsp70 homologues off. coli. The purified gene product, which we named Hsc62, clearly showed ATPase activity and was hound to a gelatin-agarose gel, from which it was specifically eluted with ATP magnesium salt. Thus, Hsc62 is similar to DnaK in this respect and probably functions as a molecular chaperon in E. coli. However, Hsc62 differs markedly from DnaK and also from Hsc66 in response to temperature: the optimum temperature for ATPase activity was increased stepwise in the order of Hsc62, Hsc66, and DnaK, Hsc66 is activated by DnaJ of E. coli in the same manner as DnaK, the natural partner protein of DnaJ. However, Hsc62 is distinct from the others: the ATPase activity of Hsc62 was not elevated by DnaJ. (C) 1998 Academic Press.

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页码：115 / 118

页数：4

相关论文

共 18 条

[1] HEAT-SHOCK PROTEINS AS MOLECULAR CHAPERONES [J].

BECKER, J ;

CRAIG, EA .

EUROPEAN JOURNAL OF BIOCHEMISTRY, 1994, 219 (1-2) :11-23

[2]

CRY DM, 1994, J BIOL CHEM, V269, P9798

[3] WHOLE-GENOME RANDOM SEQUENCING AND ASSEMBLY OF HAEMOPHILUS-INFLUENZAE RD [J].

FLEISCHMANN, RD ;

ADAMS, MD ;

WHITE, O ;

CLAYTON, RA ;

KIRKNESS, EF ;

KERLAVAGE, AR ;

BULT, CJ ;

TOMB, JF ;

DOUGHERTY, BA ;

MERRICK, JM ;

MCKENNEY, K ;

SUTTON, G ;

FITZHUGH, W ;

FIELDS, C ;

GOCAYNE, JD ;

SCOTT, J ;

SHIRLEY, R ;

LIU, LI ;

GLODEK, A ;

KELLEY, JM ;

WEIDMAN, JF ;

PHILLIPS, CA ;

SPRIGGS, T ;

HEDBLOM, E ;

COTTON, MD ;

UTTERBACK, TR ;

HANNA, MC ;

NGUYEN, DT ;

SAUDEK, DM ;

BRANDON, RC ;

FINE, LD ;

FRITCHMAN, JL ;

FUHRMANN, JL ;

GEOGHAGEN, NSM ;

GNEHM, CL ;

MCDONALD, LA ;

SMALL, KV ;

FRASER, CM ;

SMITH, HO ;

VENTER, JC .

SCIENCE, 1995, 269 (5223) :496-512

[4] Principles of chaperone-assisted protein folding: Differences between in vitro and in vivo mechanisms [J].

Frydman, J ;

Hartl, FU .

SCIENCE, 1996, 272 (5267) :1497-1502

[5] PROTEIN FOLDING IN THE CELL [J].

GETHING, MJ ;

SAMBROOK, J .

NATURE, 1992, 355 (6355) :33-45

[6] Molecular chaperones in cellular protein folding [J].

Hartl, FU .

NATURE, 1996, 381 (6583) :571-580

[7] Functional specificity among Hsp70 molecular chaperones [J].

James, P ;

Pfund, C ;

Craig, EA .

SCIENCE, 1997, 275 (5298) :387-389

[8] HSC66, AN HSP70 HOMOLOG IN ESCHERICHIA-COLI, IS INDUCED BY COLD SHOCK BUT NOT BY HEAT-SHOCK [J].

LELIVELT, MJ ;

KAWULA, TH .

JOURNAL OF BACTERIOLOGY, 1995, 177 (17) :4900-4907

[9] ROLE OF THE ESCHERICHIA-COLI DNAK AND DNAJ HEAT-SHOCK PROTEINS IN THE INITIATION OF BACTERIOPHAGE-LAMBDA-DNA REPLICATION [J].

LIBEREK, K ;

GEORGOPOULOS, C ;

ZYLICZ, M .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1988, 85 (18) :6632-6636

[10] DNAK AS A THERMOMETER - THREONINE-199 IS SITE OF AUTOPHOSPHORYLATION AND IS CRITICAL FOR ATPASE ACTIVITY [J].

MCCARTY, JS ;

WALKER, GC .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1991, 88 (21) :9513-9517