Premium
Mass spectrometric identification of a novel phosphorylation site in subunit NDUFA10 of bovine mitochondrial complex I
Author(s) -
Schilling Birgit,
Aggeler Robert,
Schulenberg Birte,
Murray James,
Row Richard H.,
Capaldi Roderick A.,
Gibson Bradford W.
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.03.061
Subject(s) - phosphorylation , phosphoprotein , phosphopeptide , serine , protein subunit , mitochondrion , protein phosphorylation , chemistry , biochemistry , microbiology and biotechnology , biology , protein kinase a , gene
Mitochondrial Complex I (NADH:ubiquinone oxidoreductase) consists of at least 46 subunits. Phosphorylation of the 42‐kDa subunit NDUFA10 was recently reported using a novel phosphoprotein stain [Schulenberg et al. (2003) Analysis of steady‐state protein phosphorylation in mitochondria using a novel fluorescent phosphosensor dye. J. Biol. Chem. 278, 27251]. Two smaller Complex I phosphoproteins, ESSS and MWFE, and their sites of modification, have since been determined [Chen et al. (2004) The phosphorylation of subunits of complex I from bovine heart mitochondria. J. Biol. Chem. 279, 26036]. Here we identify the site of phosphorylation in NDUFA10 from bovine heart mitochondria by tandem mass spectrometry. A single phosphopeptide spanning residues 47–60 was identified and confirmed by synthesis to be (47)LITVDGNICSGKpSK(60), establishing serine‐59 as the site of phosphorylation.