REGULATION OF HEAT-SHOCK FACTOR TRIMER FORMATION - ROLE OF A CONSERVED LEUCINE ZIPPER
REGULATION OF HEAT-SHOCK FACTOR TRIMER FORMATION - ROLE OF A CONSERVED LEUCINE ZIPPER
复制标题
DOI：
10.1126/science.8421783
复制
发表时间：
1993-01-08
期刊：
影响因子：
56.9
通讯作者：
WU, C
中科院分区：
文献类型：
--
作者：
RABINDRAN, SK;HAROUN, RI;WU, C
人和果蝇的热休克转录因子（HSFs）是一种多拉链蛋白，与DNA的结合受到热休克诱导的三聚体的调节。HSF三聚体的形成依赖于位于蛋白质氨基末端区域的疏水性七肽重复序列。在人HSF 1的羧基末端的两个亚区被鉴定为在正常条件下保持蛋白质的单体形式。其中之一含有在脊椎动物和昆虫HSF之间保守的亮氨酸拉链基序。这些结果表明，羧基末端拉链可以抑制形成三聚体的氨基末端HSF拉链元件通过分子内卷曲螺旋相互作用，是敏感的热休克。
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.