Promotion of mitochondrial membrane complex assembly by a proteolytically inactive yeast Lon

  • M Rep
  • , J M van Dijl
  • , K Suda
  • , G Schatz
  • , L A Grivell
  • , C K Suzuki

Research output: Contribution to journalArticleAcademicpeer-review

153 Citations (Scopus)

Abstract

Afg3p and Rca1p are adenosine triphosphate (ATP)-dependent metalloproteases in yeast mitochondria. Cells lacking both proteins exhibit defects in respiration-dependent growth, degradation of mitochondrially synthesized proteins, and assembly of inner-membrane complexes. Defects in growth and protein assembly, but not in degradation, were suppressed by overproduction of yeast mitochondrial Lon, an ATP-dependent serine protease. Suppression by Lon was enhanced by inactivation of the proteolytic site and was prevented by mutation of the ATP-binding site. It is suggested that the mitochondrial proteases Lon, Afg3p, and Rca1p can also serve a chaperone-like function in the assembly of mitochondrial protein complexes.

Original languageEnglish
Pages (from-to)103-106
Number of pages4
JournalScience
Volume274
Issue number5284
Publication statusPublished - 4-Oct-1996

Keywords

  • SACCHAROMYCES-CEREVISIAE
  • PUTATIVE ATPASES
  • PROTEIN FAMILY
  • GENE
  • MEMBER
  • ENCODES
  • CHAPERONE
  • SEQUENCE
  • BINDING
  • OXIDASE

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