TRUNCATED GROEL MONOMER HAS THE ABILITY TO PROMOTE FOLDING OF RHODANESE WITHOUT GROES AND ATP

被引：35

作者：

MAKINO, Y ^{[1
]}

TAGUCHI, H ^{[1
]}

YOSHIDA, M ^{[1
]}

机构：

[1] TOKYO INST TECHNOL,RESOURCES UTILIZAT RES LAB,NAGATSUTA 4259,YOKOHAMA,KANAGAWA 227,JAPAN

来源：

FEBS LETTERS | 1993年 / 336卷 / 02期

关键词：

CHAPERONIN; GROEL; GROES; PROTEIN FOLDING; RHODANESE;

D O I：

10.1016/0014-5793(93)80838-L

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：

Similar to chaperonins from other sources, intact chaperonin from Escherichia coli (GroEL) exists as a tetradecamer, and the ability to promote folding of other proteins has been considered to be dependent on this oligomeric structure. However, the peptide fragments of GroEL of molecular size 34-50 kDa, which are produced by limited proteolysis of monomeric GroEL and are unable to assemble into an oligomer, retain the ability to promote folding of rhodanese even though the yield of productive folding is lower than the intact GroEL/GroES/ATP system. This promotion by truncated GroEL obeys rapid kinetics and does not require GroES and ATP.

引用

页码：363 / 367

页数：5

共 29 条

[1] A CHAPERONIN PROTEIN MODULE INVOLVED IN RECOGNITION OF INTERACTIVE PROTEIN SURFACES [J].

ALCONADA, A ;

CUEZVA, JM .

TRENDS IN BIOCHEMICAL SCIENCES, 1993, 18 (03) :81-82

[2]

BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3

[3] CLONING, SEQUENCE-ANALYSIS, AND EXPRESSION OF ALTERATION OF THE MESSENGER-RNA STABILITY GENE (AMS+) OF ESCHERICHIA-COLI [J].

CHANDA, PK ;

ONO, M ;

KUWANO, M ;

KUNG, HF .

JOURNAL OF BACTERIOLOGY, 1985, 161 (01) :446-449

[4] PROTEINS AS MOLECULAR CHAPERONES [J].

ELLIS, J .

NATURE, 1987, 328 (6129) :378-379

[5]

ELLIS RJ, 1991, ANNU REV BIOCHEM, V60, P321, DOI 10.1146/annurev.bi.60.070191.001541

[6] THE EMERGENCE OF THE CHAPERONE MACHINES [J].

GEORGOPOULOS, C .

TRENDS IN BIOCHEMICAL SCIENCES, 1992, 17 (08) :295-299

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

GETHING, MJ ;

SAMBROOK, J .

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

[8] PROTEIN FOLDING IN THE CELL - THE ROLE OF MOLECULAR CHAPERONES HSP70 AND HSP60 [J].

HARTL, FU ;

MARTIN, J ;

NEUPERT, W .

ANNUAL REVIEW OF BIOPHYSICS AND BIOMOLECULAR STRUCTURE, 1992, 21 :293-322

[9] HOMOLOGOUS PLANT AND BACTERIAL PROTEINS CHAPERONE OLIGOMERIC PROTEIN ASSEMBLY [J].

HEMMINGSEN, SM ;

WOOLFORD, C ;

VANDERVIES, SM ;

TILLY, K ;

DENNIS, DT ;

GEORGOPOULOS, CP ;

HENDRIX, RW ;

ELLIS, RJ .

NATURE, 1988, 333 (6171) :330-334

[10] PURIFICATION AND PROPERTIES OF GROE, A HOST PROTEIN INVOLVED IN BACTERIOPHAGE ASSEMBLY [J].

HENDRIX, RW .

JOURNAL OF MOLECULAR BIOLOGY, 1979, 129 (03) :375-392

← 1 2 3 →