Functional analysis of human metaxin in mitochondrial protein import in cultured cells and its relationship with the Tom complex

Khaleque Md Abdul, Kazutoyo Terada, Masato Yano, Michael T. Ryan, Illo Streimann, Nicholas J. Hoogenraad, Masataka Mori

Research output: Contribution to journalArticleResearchpeer-review

31 Citations (Scopus)

Abstract

Metaxin is an outer membrane protein of mammalian mitochondria which is suggested to be involved in protein import into the organelle. RNA blot analysis showed that distribution of metaxin mRNA in human tissues differs from that of mRNA for the translocase component Tom20. Effect of overexpression of human metaxin on mitochondrial preprotein import and processing in COS-7 cells was studied. Overexpression of metaxin resulted in impaired mitochondrial import of natural and chimeric preproteins and in their accumulation. We previously reported that overexpression of Tom20 in cultured cells causes inhibition of import of mitochondrial preprotein. Coexpression of metaxin with Tom20 had no further effect on the preprotein import. Overexpression of the cytosolic domain of metaxin also caused inhibition of preprotein import, although less strongly than the full-length metaxin. In blue native PAGE, Tom40, Tom22, and a portion of Tom20 migrated as a cornplex of ~400 kDa, and the other portion of Tom20 migrated in smaller forms of ~100 and ~40 kDa. On the other hand, metaxin migrated at a position of ~50 kDa. These results confirm earlier in vitro results that metaxin participates in preprotein import into mammalian mitochondria, and indicates that it does not associate with the Tom complex. (C) 2000 Academic Press.

Original languageEnglish
Pages (from-to)1028-1034
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume276
Issue number3
DOIs
Publication statusPublished - 5 Oct 2000
Externally publishedYes

Keywords

  • Metaxin
  • Mitochondria
  • Preprotein
  • Protein import
  • Tom complex

Cite this