[HTML][HTML] Mass spectrometric identification of a novel phosphorylation site in subunit NDUFA10 of bovine mitochondrial complex I
B Schilling, R Aggeler, B Schulenberg, J Murray… - FEBS letters, 2005 - Elsevier
B Schilling, R Aggeler, B Schulenberg, J Murray, RH Row, RA Capaldi, BW Gibson
FEBS letters, 2005•ElsevierMitochondrial 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. 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 …
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.
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