A NOVEL ATPASE COMPLEX SELECTIVELY ACCUMULATED UPON HEAT-SHOCK IS A MAJOR CELLULAR-COMPONENT OF THERMOPHILIC ARCHAEBACTERIA

被引：168

作者：

PHIPPS, BM ^{[1
]}

HOFFMANN, A ^{[1
]}

STETTER, KO ^{[1
]}

BAUMEISTER, W ^{[1
]}

机构：

[1] UNIV REGENSBURG,DEPT MICROBIOL,W-8400 REGENSBURG,GERMANY

来源：

EMBO JOURNAL | 1991年 / 10卷 / 07期

关键词：

ATPASE; HEAT SHOCK PROTEIN; PROTEIN STRUCTURE; RING-SHAPED COMPLEX; THERMOPHILIC ARCHAEBACTERIA;

D O I：

10.1002/j.1460-2075.1991.tb07695.x

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 discovered a large cylindrical protein complex which is an abundant component of the cytoplasm of extremely thermophilic archaebacteria. Structural analysis by image processing of electron micrographs suggests that the complex is composed of two stacked rings of eight subunits each; the rings enclose a central channel. The complex purified from the hyperthermophile Pyrodictium occultum is composed of equal quantities of two polypeptides Of M(r) 56 000 and 59 000. It exhibits an extremely thermostable ATPase activity with a temperature optimum of 100-degrees-C. The basal level of the ATPase complex in the cell is high, and it becomes highly enriched as a result of heat shock (shift from 102-degrees-C to 108-degrees-C) or balanced growth at temperatures near the physiological upper limit. Immunoblotting results indicate that a related protein is present in most thermophilic archaebacteria and in Escherichia coli. This protein complex may play an important role in the adaptation of thermophilic archaebacteria to life at high temperature.

引用

页码：1711 / 1722

页数：12

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