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Mitochondrial import of the human chaperonin (HSP60) protein

Authors
Journal
Biochemical and Biophysical Research Communications
0006-291X
Publisher
Elsevier
Publication Date
Volume
169
Issue
2
Identifiers
DOI: 10.1016/0006-291x(90)90344-m
Disciplines
  • Biology

Abstract

Abstract The mitochondrial import of a member of the “chaperonin” group of proteins which play an essential role in the import of protein into organelles and their subsequent proper folding has been examined. The cDNA for human hsp60 (synonyms: GroEL homolog, P1) was transcribed and translated in vitro and its import into isolated rat heart mitochondria examined. The protein was converted into a mature form of lower molecular mass (≈ 58 kDa) which was resistant to trypsin treatment. The import of human hsp60 into mitochondria was inhibited in the presence of an uncoupler and also no import occurred when the N-terminal presequence was lacking. These results indicate that the chaperonin protein(s) are transported into mitochondria by a process similar to other imported mitochondrial proteins. Our results also indicate that although the P1 protein precursor was efficiently imported into mitochondria, in comparison to precursors of other mitochondrial proteins (viz. ornithine carbamoyltransferase and uncoupling protein) much less binding of pre P1 to mitochondria was observed. The significance of this latter observation at present is unclear.

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