Effect of single point mutations in citrate synthase on binding to GroEL

被引：12

作者：

Zahn, R ^{[1
]}

Lindner, P ^{[1
]}

Axmann, SE ^{[1
]}

Pluckthun, A ^{[1
]}

机构：

[1] UNIV ZURICH,INST BIOCHEM,CH-8057 ZURICH,SWITZERLAND

来源：

FEBS LETTERS | 1996年 / 380卷 / 1-2期

关键词：

molecular chaperone; protein folding; protein stability; GroEL; pre-beta-lactamase; citrate synthase;

D O I：

10.1016/0014-5793(96)00013-0

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：

Six single point mutants of yeast citrate synthase were analyzed for binding to the molecular chaperone GroEL. In contrast to the mild-type and G276S, all other G276-mutants were able to displace pre-beta-lactamase from GroEL. The off-rate constant for pre-beta-lactamase must be at least partially rate-limiting, leading to an equilibrium dissociation constant between 10(-10) M and 10(-12)M. Direct evidence for binding of citrate synthase was obtained from gel filtration experiments, The results suggest that thermodynamic rather than structural features of the mutants determine the degree of binding to the chaperone.

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收藏

页码：152 / 156

页数：5

相关论文

共 38 条

[1] THE CRYSTAL-STRUCTURE OF THE BACTERIAL CHAPERONIN GROEL AT 2.8-ANGSTROM [J].

BRAIG, K ;

OTWINOWSKI, Z ;

HEGDE, R ;

BOISVERT, DC ;

JOACHIMIAK, A ;

HORWICH, AL ;

SIGLER, PB .

NATURE, 1994, 371 (6498) :578-586

[2] GROE FACILITATES REFOLDING OF CITRATE SYNTHASE BY SUPPRESSING AGGREGATION [J].

BUCHNER, J ;

SCHMIDT, M ;

FUCHS, M ;

JAENICKE, R ;

RUDOLPH, R ;

SCHMID, FX ;

KIEFHABER, T .

BIOCHEMISTRY, 1991, 30 (06) :1586-1591

[3]

CHANDRASEKHAR GN, 1986, J BIOL CHEM, V261, P2414

[4] LOCATION OF A FOLDING PROTEIN AND SHAPE CHANGES IN GROEL-GROES COMPLEXES IMAGED BY CRYOELECTRON MICROSCOPY [J].

CHEN, S ;

ROSEMAN, AM ;

HUNTER, AS ;

WOOD, SP ;

BURSTON, SG ;

RANSON, NA ;

CLARKE, AR ;

SAIBIL, HR .

NATURE, 1994, 371 (6494) :261-264

[5] THE FOLDING OF GROEL-BOUND BARNASE AS A MODEL FOR CHAPERONIN-MEDIATED PROTEIN-FOLDING [J].

CORRALES, FJ ;

FERSHT, AR .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1995, 92 (12) :5326-5330

[6] THE GROES AND GROEL HEAT-SHOCK GENE-PRODUCTS OF ESCHERICHIA-COLI ARE ESSENTIAL FOR BACTERIAL-GROWTH AT ALL TEMPERATURES [J].

FAYET, O ;

ZIEGELHOFFER, T ;

GEORGOPOULOS, C .

JOURNAL OF BACTERIOLOGY, 1989, 171 (03) :1379-1385

[7] RESIDUES IN CHAPERONIN GROEL REQUIRED FOR POLYPEPTIDE BINDING AND RELEASE [J].

FENTON, WA ;

KASHI, Y ;

FURTAK, K ;

HORWICH, AL .

NATURE, 1994, 371 (6498) :614-619

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

GETHING, MJ ;

SAMBROOK, J .

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

[9] RECONSTITUTION OF ACTIVE DIMERIC RIBULOSE BISPHOSPHATE CARBOXYLASE FROM AN UNFOLDED STATE DEPENDS ON 2 CHAPERONIN PROTEINS AND MG-ATP [J].

GOLOUBINOFF, P ;

CHRISTELLER, JT ;

GATENBY, AA ;

LORIMER, GH .

NATURE, 1989, 342 (6252) :884-889

[10] REFOLDING OF BARNASE MUTANTS AND PRO-BARNASE IN THE PRESENCE AND ABSENCE OF GROEL [J].

GRAY, TE ;

EDER, J ;

BYCROFT, M ;

DAY, AG ;

FERSHT, AR .

EMBO JOURNAL, 1993, 12 (11) :4145-4150

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