Abstract：
: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.
journal_name
Celljournal_title
Cellauthors
Caplan AJ,Cyr DM,Douglas MGdoi
10.1016/s0092-8674(05)80063-7subject
Has Abstractpub_date
1992-12-24 00:00:00pages
1143-55issue
7eissn
0092-8674issn
1097-4172pii
S0092-8674(05)80063-7journal_volume
71pub_type
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