A mitochondrial homolog of bacterial GrpE interacts with mitochondrial hsp70 and is essential for viability.

作者: L. Bolliger , O. Deloche , B.S. Glick , C. Georgopoulos , P. Jenö

DOI: 10.1002/J.1460-2075.1994.TB06469.X

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摘要: Mitochondrial hsp70 (mhsp70) is located in the matrix and an essential component of mitochondrial protein import system. To study function mhsp70 to identify possible partner proteins we constructed a yeast strain which all molecules carry C-terminal hexa-histidine tag. The tagged appears be functional vivo. When ATP depleted extract was incubated with nickel-derivatized affinity resin, resin bound not only mhsp70, but also 23 kDa protein. This dissociated from by ATP. ADP GTP were much less effective promoting dissociation whereas CTP TTP inactive. We cloned gene encoding gene, termed GRPE, encodes 228 residue protein, whose sequence closely resembles that bacterial GrpE Microsequencing purified established it as product GRPE gene. Yeast GrpEp made precursor cleaved upon into isolated mitochondria. for viability. suggest this interacts manner analogous DnaK E.coli.

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