Complementation between mitochondrial processing peptidase (MPP) subunits from different species

Jiri Adamec, Olexandre Gakh, Jaroslav Spizek, Frantisek Kalousek

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

Mitochondrial processing peptidase (MPP), a dimer of nonidentical subunits, is the primary peptidase responsible for the removal of leader peptides from nuclearly encoded mitochondrial proteins. Alignments of the α and β subunits of MPP (α- and β-MPP) from different species show strong protein sequence similarity in certain regions, including a highly negatively charged region as well as a domain containing a putative metal ion binding site. In this report, we describe experiments in which we combine the subunits of MPP from yeast, rat, and Neurospora crassa, both in vivo and in vitro and mesure the resultant processing activity. For in vivo complementation, we used the temperature sensitive mif1 and mif2 yeast mutants, which lack MPP activity at the nonpermissive temperature (37°C). We found that the defective α-MPP of mif2 cannot be substituted for by the α- MPP from rat or Neurospora. On the other hand, the β-MPP from rat and Neurospora can fully substitute for the defective β-MPP in the mif1 mutant. These results were confirmed in in vitro experiments in which individually expressed subunits were combined. Only combinations of the α-MPP from yeast with the β-MPP from rat or Neurospora produced active MPP.

Original languageEnglish (US)
Pages (from-to)77-85
Number of pages9
JournalArchives of Biochemistry and Biophysics
Volume370
Issue number1
DOIs
StatePublished - Oct 1 1999

Fingerprint

Neurospora
Rats
Yeast
Yeasts
mitochondrial processing peptidase
Neurospora crassa
Temperature
Mitochondrial Proteins
Protein Sorting Signals
Dimers
Metal ions
Peptide Hydrolases
Metals
Experiments
Binding Sites
Ions
Processing
Proteins
In Vitro Techniques

Keywords

  • Interspecies complementation
  • Mitochondrial processing peptidase (MPP)
  • Transport
  • Yeast

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

Cite this

Complementation between mitochondrial processing peptidase (MPP) subunits from different species. / Adamec, Jiri; Gakh, Olexandre; Spizek, Jaroslav; Kalousek, Frantisek.

In: Archives of Biochemistry and Biophysics, Vol. 370, No. 1, 01.10.1999, p. 77-85.

Research output: Contribution to journalArticle

Adamec, Jiri ; Gakh, Olexandre ; Spizek, Jaroslav ; Kalousek, Frantisek. / Complementation between mitochondrial processing peptidase (MPP) subunits from different species. In: Archives of Biochemistry and Biophysics. 1999 ; Vol. 370, No. 1. pp. 77-85.
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