Analysis of the soluble ATP-binding proteome of plant mitochondria identifies new proteins and nucleotide triphosphate interactions within the matrix

J Proteome Res. 2006 Dec;5(12):3459-69. doi: 10.1021/pr060403j.

Abstract

The interactions of ATP inside plant mitochondria were investigated by identifying the soluble nucleotide binding proteome captured using immobilized ATP. Selected proteins were separated by 1D SDS-PAGE and 2D IEF-SDS-PAGE and identified by ESI-Q-TOF MS/MS. A range of highly enriched proteins were identified from the mitochondrial proteome, including 14-3-3 proteins and RNA binding proteins, as well as proteins known to contain nucleotide binding domains and/or to be inhibited or stimulated by ATP.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ATP-Binding Cassette Transporters / analysis
  • ATP-Binding Cassette Transporters / metabolism*
  • Adaptor Proteins, Signal Transducing / analysis
  • Adaptor Proteins, Signal Transducing / metabolism
  • Arabidopsis / chemistry*
  • Chromatography, Affinity
  • Electrophoresis, Polyacrylamide Gel
  • Mass Spectrometry
  • Mitochondria / chemistry*
  • Mitochondrial Proteins / analysis*
  • Mitochondrial Proteins / metabolism
  • Plant Proteins / analysis*
  • Plant Proteins / metabolism
  • Proteomics*

Substances

  • ATP-Binding Cassette Transporters
  • Adaptor Proteins, Signal Transducing
  • Mitochondrial Proteins
  • Plant Proteins