Mitochondrial localization of AtOXA1, an Arabidopsis homologue of yeast Oxa1p involved in the insertion and assembly of protein complexes in mitochondrial inner membrane

Wataru Sakamoto, Nathalie Spielewoy, Géraldine Bonnard, Minoru Murata, Henri Wintz

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

Components of some protein complexes present in the inner membrane of mitochondria are encoded in both nuclear and mitochondrial genomes, and correct sorting and assembly of these proteins is necessary for proper respiratory function. Recent studies in yeast suggest that Oxa1p, a protein conserved between prokaryotes and eukaryotes, is an essential factor for protein sorting and assembly into membranes. We previously identified AtOXA1, an Arabidopsis homologue of OXA1 by functional complementation of a yeast oxa1- mutant. In this study, we investigated the genomic organization of AtOXA1 and localization of the AtOXA1 protein. Characterization of the AtOXA1 genomic region indicated that the gene consists of 10 exons and is located on chromosome V. A database search also revealed another gene coding for a putative protein homologous to AtOXA1 on chromosome II. Transient expression of a green fluorescent protein (GFP) fusion in suspension-cultured tobacco cells showed that AtOXA1 is targeted into mitochondria by its N-terminal presequence. Antibodies raised against AtOXA1 recognized a 38-kDa intrinsic protein of the inner mitochondrial membrane. Thus, localization of AtOXA1 in the mitochondrial inner membrane, together with our previous complementation experiment in yeast, suggested that it is a functional homologue of Oxa1p.

Original languageEnglish
Pages (from-to)1157-1163
Number of pages7
JournalPlant and Cell Physiology
Volume41
Issue number10
DOIs
Publication statusPublished - Jan 1 2000

Keywords

  • Arabidopsis thaliana
  • Green fluorescent protein (GFP)
  • Inner membrane
  • Mitochondria
  • OXA1

ASJC Scopus subject areas

  • Physiology
  • Plant Science
  • Cell Biology

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