Plant mitochondrial nucleoside diphosphate kinase is attached to the membrane through interaction with the adenine nucleotide translocator

FEBS Lett. 2003 Dec 4;555(2):363-6. doi: 10.1016/s0014-5793(03)01288-2.

Abstract

This study shows that the plant mitochondrial nucleoside diphosphate kinase (mNDPK) localizes to both the intermembrane space and to the mitochondrial inner membrane. We show that mNDPK is very firmly attached to the membrane. Co-immunoprecipitation experiments identified the adenine nucleotide translocator as an interaction partner. This is the first report showing a direct association between these two proteins, although previous studies have shown metabolic cooperation between them. Possible consequences for mitochondrial energy metabolism are discussed.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Intracellular Membranes / metabolism*
  • Membrane Proteins / metabolism
  • Mitochondria / enzymology*
  • Mitochondrial ADP, ATP Translocases / metabolism*
  • Molecular Sequence Data
  • Nucleoside-Diphosphate Kinase / chemistry
  • Nucleoside-Diphosphate Kinase / metabolism*
  • Pisum sativum / enzymology
  • Precipitin Tests
  • Solubility

Substances

  • Membrane Proteins
  • Mitochondrial ADP, ATP Translocases
  • Nucleoside-Diphosphate Kinase