REGULATION OF HEAT-SHOCK FACTOR TRIMER FORMATION - ROLE OF A CONSERVED LEUCINE ZIPPER

被引：416

作者：

RABINDRAN, SK ^{[1
]}

HAROUN, RI ^{[1
]}

CLOS, J ^{[1
]}

WISNIEWSKI, J ^{[1
]}

WU, C ^{[1
]}

机构：

[1] NCI,BIOCHEM LAB,BETHESDA,MD 20892

来源：

SCIENCE | 1993年 / 259卷 / 5092期

关键词：

D O I：

10.1126/science.8421783

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

The human and Drosophila heat shock transcription factors (HSFs) are multi-zipper proteins with high-affinity binding to DNA that is regulated by heat shock-induced trimerization. Formation of HSF trimers is dependent on hydrophobic heptad repeats located in the amino-terminal region of the protein. Two subregions at the carboxyl-terminal end of human HSF1 were identified that maintain the monomeric form of the protein under normal conditions. One of these contains a leucine zipper motif that is conserved between vertebrate and insect HSFs. These results suggest that the carboxyl-terminal zipper may suppress formation of trimers by the amino-terminal HSF zipper elements by means of intramolecular coiled-coil interactions that are sensitive to heat shock.

引用

页码：230 / 234

页数：5

共 38 条

[1] THE HUMAN HEAT-SHOCK PROTEIN HSP70 INTERACTS WITH HSF, THE TRANSCRIPTION FACTOR THAT REGULATES HEAT-SHOCK GENE-EXPRESSION [J].