Analysis of the soluble ATP-binding proteome of plant mitochondria identifies new proteins and nucleotide triphosphate interactions within the matrix.
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.
Ito
Jun
J
ARC Centre of Excellence in Plant Energy Biology and School of Biomedical, Biomolecular and Chemical Sciences, The University of Western Australia, 35 Stirling Highway, M316, Crawley 6009, WA, Australia.
Heazlewood
Joshua L
JL
Millar
A Harvey
AH
D018528:ATP-Binding Cassette Transporters / Q000032:analysis / Q000378:metabolism*; D048868:Adaptor Proteins, Signal Transducing / Q000032:analysis / Q000378:metabolism; D017360:Arabidopsis / Q000737:chemistry*; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D013058:Mass Spectrometry; D008928:Mitochondria / Q000737:chemistry*; D024101:Mitochondrial Proteins / Q000032:analysis* / Q000378:metabolism; D010940:Plant Proteins / Q000032:analysis* / Q000378:metabolism; D040901:Proteomics
D018528:ATP-Binding Cassette Transporters; D048868:Adaptor Proteins, Signal Transducing; D024101:Mitochondrial Proteins; D010940:Plant Proteins