Biochemical and physiological studies of a small heat shock protein from a lactic acid bacterium.

被引：2

作者：

Delmas, F ^{[1
]}

Diviès, C ^{[1
]}

Guzzo, J ^{[1
]}

机构：

[1] ENSBANA, UA, INRA, Microbiol Lab, F-21000 Dijon, France

来源：

SCIENCES DES ALIMENTS | 2000年 / 20卷 / 01期

关键词：

Oenococcus oeni; stress; small heat shock protein; chaperone;

D O I：

10.3166/sda.20.111-117

中图分类号：

TS2 [食品工业];

学科分类号：

0832 ;

摘要：

Oenococcus oeni is the lactic acid bacterium mostly responsible for malolactic fermentation in wine. Among the major heat shock proteins from O. oeni, the synthesis of the 18 kDa protein called Lo18 was found to be markedly induced in several kinds of stress and during stationary growth phase. Cellular fractionation and Western Blot showed that Lo18 is peripherally associated with the membrane in O. oeni. Furthermore, non denaturing gel electrophoresis showed that Lo18 assembles into multimeric structures of three or more subunits. Lo18 was purified and in vitro chaperone activity was showed. This activity is characterised by a diminution of citrate synthase thermal aggregation.

引用

页码：111 / 117

页数：7

共 13 条

[1] Refolding chromatography with immobilized mini-chaperones [J].

Altamirano, MM ;

Golbik, R ;

Zahn, R ;

Buckle, AM ;

Fersht, AR .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (08) :3576-3578

[2] MOLECULAR-WEIGHT ESTIMATIONS OF PROTEINS BY ELECTROPHORESIS IN POLYACRYLAMIDE GELS OF GRADED POROSITY [J].

ANDERSSON, LO ;

BORG, H ;

MIKAELSSON, M .

FEBS LETTERS, 1972, 20 (02) :199-+

[3] Mycobacterium tuberculosis 16-kDa antigen (Hsp16.3) functions as an oligomeric structure in vitro to suppress thermal aggregation [J].

Chang, ZY ;

Primm, TP ;

Jakana, J ;

Lee, IH ;

Serysheva, I ;

Chiu, W ;

Gilbert, HF ;

Quiocho, FA .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1996, 271 (12) :7218-7223

[4] Stabilization of proteins and peptides in diagnostic immunological assays by the molecular chaperone Hsp25 [J].

Ehrnsperger, M ;

Hergersberg, C ;

Wienhues, U ;

Nichtl, A ;

Buchner, J .

ANALYTICAL BIOCHEMISTRY, 1998, 259 (02) :218-225

[5] CLONING OF THE PSEUDOMONAS-AERUGINOSA ALKALINE PROTEASE GENE AND SECRETION OF THE PROTEASE INTO THE MEDIUM BY ESCHERICHIA-COLI [J].

GUZZO, J ;

MURGIER, M ;

FILLOUX, A ;

LAZDUNSKI, A .

JOURNAL OF BACTERIOLOGY, 1990, 172 (02) :942-948

[6] A small heat shock protein from Leuconostoc oenos induced by multiple stresses and during stationary growth phase [J].

Guzzo, J ;

Delmas, F ;

Pierre, F ;

Jobin, MP ;

Samyn, B ;

VanBeeumen, J ;

Cavin, JF ;

Divies, C .

LETTERS IN APPLIED MICROBIOLOGY, 1997, 24 (05) :393-396

[7] Membrane physical state controls the signaling mechanism of the heat shock response in Synechocystis PCC 6803:: Identification of hsp17 as a "fluidity gene" [J].

Horváth, I ;

Glatz, A ;

Varvasovszki, V ;

Török, Z ;

Páli, T ;

Balogh, G ;

Kovács, E ;

Nádasdi, L ;

Benkö, S ;

Joó, F ;

Vígh, L .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (07) :3513-3518

[8] ALPHA-CRYSTALLIN CAN FUNCTION AS A MOLECULAR CHAPERONE [J].

HORWITZ, J .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1992, 89 (21) :10449-10453

[9] Molecular characterization of the gene encoding an 18-kilodalton small heat shock protein associated with the membrane of Leuconostoc oenos [J].

Jobin, MP ;

Delmas, F ;

Garmyn, D ;

Divies, C ;

Guzzo, J .

APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 1997, 63 (02) :609-614

[10] CLEAVAGE OF STRUCTURAL PROTEINS DURING ASSEMBLY OF HEAD OF BACTERIOPHAGE-T4 [J].

LAEMMLI, UK .

NATURE, 1970, 227 (5259) :680-+

← 1 2 →