YDJ1P FACILITATES POLYPEPTIDE TRANSLOCATION ACROSS DIFFERENT INTRACELLULAR MEMBRANES BY A CONSERVED MECHANISM
YDJ1P FACILITATES POLYPEPTIDE TRANSLOCATION ACROSS DIFFERENT INTRACELLULAR MEMBRANES BY A CONSERVED MECHANISM
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DOI：
10.1016/s0092-8674(05)80063-7
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发表时间：
1992-12-24
期刊：
影响因子：
64.5
通讯作者：
DOUGLAS, MG
中科院分区：
文献类型：
--
作者：
CAPLAN, AJ;CYR, DM;DOUGLAS, MG
S的作用。研究了酿酒酵母YDJ 1蛋白（YDJ 1 p）在多肽跨膜转运中的作用。一种条件性的p53 j1突变株（p53 j1 - 151 TS）在37 ℃下不能将几种多肽输入线粒体和α因子输入内质网。这些缺陷被E. coli dnaJ或过量表达S.酿酒酵母SIS 1蛋白另一种不能被法尼基化的突变体（S406）表现出与S401 -151菌株相似的转运缺陷。此外，与野生型蛋白相比，纯化的p53 j1 - 151 p刺激hsp 70 SSA 1的ATP酶活性的能力大大降低。总之，这些数据表明，YDJ 1 p的功能在多肽易位中的一种保守的方式，可能在细胞器膜和协会与热休克蛋白70蛋白。
The role of S. cerevisiae YDJ1 protein (YDJ1p) in polypeptide translocation across membranes has been examined. A conditional ydj1 mutant strain (ydj1-151TS) is defective for import of several polypeptides into mitochondria and alpha factor into the endoplasmic reticulum at 37-degrees-C. These defects are suppressed by E. coli dnaJ or overexpression of S. cerevisiae SIS1 proteins. A different ydj1 mutant, which cannot be farnesylated (ydj1-S406), displays similar transport defects to the ydj1-151 strain. Furthermore, the ability of purified ydj1-151p to stimulate the ATPase activity of hsp70SSA1 was greatly diminished compared with the wild-type protein. Together, these data suggest that YDJ1p functions in polypeptide translocation in a conserved manner, probably acting at organelle membranes and in association with hsp70 proteins.