The J domain-related cochaperone Tim16 is a constituent of the mitochondrial TIM23 preprotein translocase

Nat Struct Mol Biol. 2004 Mar;11(3):234-41. doi: 10.1038/nsmb734. Epub 2004 Feb 15.

Abstract

Mitochondria import the vast majority of their proteins from the cytosol. The mitochondrial import motor of the TIM23 translocase drives the translocation of precursor proteins across the outer and inner membrane in an ATP-dependent reaction. Tim44 at the inner face of the translocation pore recruits the chaperone mtHsp70, which binds the incoming precursor protein. This reaction is assisted by the cochaperones Tim14 and Mge1. We have identified a novel essential cochaperone, Tim16. It is related to J-domain proteins and forms a stable subcomplex with the J protein Tim14. Depletion of Tim16 has a marked effect on protein import into the mitochondrial matrix, impairs the interaction of Tim14 with the TIM23 complex and leads to severe structural changes of the import motor. In conclusion, Tim16 is a constituent of the TIM23 preprotein translocase, where it exerts crucial functions in the import motor.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Fungal Proteins
  • Intracellular Membranes / metabolism
  • Membrane Transport Proteins / metabolism*
  • Mitochondria / metabolism
  • Mitochondria / ultrastructure
  • Mitochondrial Membrane Transport Proteins
  • Mitochondrial Proteins / metabolism*
  • Molecular Motor Proteins / metabolism
  • Protein Binding
  • Protein Precursors / metabolism
  • Protein Transport
  • Saccharomyces cerevisiae Proteins / metabolism*

Substances

  • Fungal Proteins
  • Membrane Transport Proteins
  • Mitochondrial Membrane Transport Proteins
  • Mitochondrial Proteins
  • Molecular Motor Proteins
  • Pam16 protein, S cerevisiae
  • Protein Precursors
  • Saccharomyces cerevisiae Proteins
  • TIM23 protein, S cerevisiae
  • Tim14 protein, S cerevisiae