The mitochondrial protein translocation motor: Structural conservation between the human and yeast tim14/pam18- tim16/pam16 co-chaperones

Shira Elsner, Dana Simian, Ohad Iosefson, Milit Marom, Abdussalam Azem*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

Most of our knowledge regarding the process of protein import into mitochondria has come from research employing Saccharomyces cerevisiae as a model system. Recently, several mammalian homologues of the mitochondrial motor proteins were identified. Of particular interest for us is the human Tim14/Pam18-Tim16/Pam16 complex. We chose a structural approach in order to examine the evolutionary conservation between yeast Tim14/Pam18-Tim16/Pam16 proteins and their human homologues. For this purpose, we examined the structural properties of the purified human proteins and their interaction with their yeast homologues, in vitro. Our results show that the soluble domains of the human Tim14/Pam18 and Tim16/Pam16 proteins interact with their yeast counterparts, forming heterodimeric complexes and that these complexes interact with yeast mtHsp70.

Original languageEnglish
Pages (from-to)2041-2053
Number of pages13
JournalInternational Journal of Molecular Sciences
Volume10
Issue number5
DOIs
StatePublished - May 2009

Keywords

  • MtHsp70
  • Tim14 (also known as Pam18)
  • Tim16 (also known as Pam16)
  • Translocation motor

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