Article

  • The EMBO Journal (2003) 22, 5951 - 5961
  • doi:10.1093/emboj/cdg566

Mss51p promotes mitochondrial Cox1p synthesis and interacts with newly synthesized Cox1p

Xochitl Perez-Martinez1, Sarah A. Broadley1 and Thomas D. Fox1

  1. Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853-2703, USA

Correspondence to:

Thomas D. Fox, E-mail: tdf1@cornell.edu

Received 12 June 2003; Accepted 8 September 2003; Revised 13 July 2003


The post-transcriptional role of Mss51p in mitochondrial gene expression is of great interest since MSS51 mutations suppress the respiratory defect caused by shy1 mutations. SHY1 is a Saccharomyces cerevisiae homolog of human SURF1, which when mutated causes a cytochrome oxidase assembly defect. We found that MSS51 is required for expression of the mitochondrial reporter gene ARG8mARG8m when it is inserted at the COX1 locus, but not when it is at COX2 or COX3. Unlike the COX1 mRNA-specific translational activator PET309, MSS51 has at least two targets in COX1 mRNA. MSS51 acts in the untranslated regions of the COX1 mRNA, since it was required to synthesize Arg8p when ARG8m completely replaced the COX1 codons. MSS51 also acts on a target specified by the COX1 coding region, since it was required to translate either COX1 or COX1:: ARG8m coding sequences from an ectopic COX2 locus. Mss51p was found to interact physically with newly synthesized Cox1p, suggesting that it could coordinate Cox1p synthesis with insertion into the inner membrane or cytochrome oxidase assembly.

  • Keywords:

    • cytochrome c oxidase,
    • mitochondrial DNA,
    • translation,
    • untranslated regions