Pam17 and Tim44 act sequentially in protein import into the mitochondrial matrix

Import of proteins into the matrix is driven by the Tim23 presequence translocase-associated import motor PAM. The core component of PAM is the mitochondrial chaperone mtHsp70, which ensures efficient translocation of proteins across the inner membrane through interactions with the J-protein complex...

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Veröffentlicht in:The international journal of biochemistry & cell biology 2009-11, Vol.41 (11), p.2343-2349
1. Verfasser: Schiller, Dirk
Format: Artikel
Sprache:eng
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Zusammenfassung:Import of proteins into the matrix is driven by the Tim23 presequence translocase-associated import motor PAM. The core component of PAM is the mitochondrial chaperone mtHsp70, which ensures efficient translocation of proteins across the inner membrane through interactions with the J-protein complex Pam16–Pam18 (Tim16–Tim14) and its cochaperone Tim44. The recently identified non-essential Pam17 is a further member of PAM. Genetic and biochemical analyses reveal synthetic interactions between PAM17 and TIM44. Pam17 is involved in an early stage of protein translocation whereas Tim44 assists in a later step of transport, suggesting that both proteins can cooperate in a complementary manner in protein import.
ISSN:1357-2725
1878-5875
DOI:10.1016/j.biocel.2009.06.011