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Originally published In Press as doi:10.1074/mcp.M300014-MCP200 on February 22, 2003.
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Molecular & Cellular Proteomics 2:117-126, 2003.
© 2003 by The American Society for Biochemistry and Molecular Biology, Inc.

Research

Analysis of the Subunit Composition of Complex I from Bovine Heart Mitochondria*,S

Joe Carroll, Ian M. Fearnley, Richard J. Shannon, Judy Hirst and John E. Walker{ddagger}

From the Medical Research Council Dunn Human Nutrition Unit, The Wellcome Trust/MRC Building, Hills Road, Cambridge CB2 2XY, United Kingdom

Complex I purified from bovine heart mitochondria is a multisubunit membrane-bound assembly. In the past, seven of its subunits were shown to be products of the mitochondrial genome, and 35 nuclear encoded subunits were identified. The complex is L-shaped with one arm in the plane of the membrane and the other lying orthogonal to it in the mitochondrial matrix. With mildly chaotropic detergents, the intact complex has been resolved into various subcomplexes. Subcomplex I{lambda} represents the extrinsic arm, subcomplex I{alpha} consists of subcomplex I{lambda} plus part of the membrane arm, and subcomplex Iß is another substantial part of the membrane arm. The intact complex and these three subcomplexes have been subjected to extensive reanalysis. Their subunits have been separated by three independent methods (one-dimensional SDS-PAGE, two-dimensional isoelectric focusing/SDS-PAGE, and reverse phase high pressure liquid chromatography (HPLC)) and analyzed by tryptic peptide mass fingerprinting and tandem mass spectrometry. The masses of many of the intact subunits have also been measured by electrospray ionization mass spectrometry and have provided valuable information about post-translational modifications. The presence of the known 35 nuclear encoded subunits in complex I has been confirmed, and four additional nuclear encoded subunits have been detected. Subunits B16.6, B14.7, and ESSS were discovered in the SDS-PAGE analysis of subcomplex I{lambda}, in the two-dimensional gel analysis of the intact complex, and in the HPLC analysis of subcomplex Iß, respectively. Despite many attempts, no sequence information has been obtained yet on a fourth new subunit (mass 10,566 ± 2 Da) also detected in the HPLC analysis of subcomplex Iß. It is unlikely that any more subunits of the bovine complex remain undiscovered. Therefore, the intact enzyme is a complex of 46 subunits, and, assuming there is one copy of each subunit in the complex, its mass is 980 kDa.

{ddagger} To whom correspondence should be addressed: Medical Research Council Dunn Human Nutrition Unit, The Wellcome Trust/MRC Bldg., Hills Rd., Cambridge CB2 2XY, UK. Tel.: 44-1223-252701; Fax: 44-1223-252705; E-mail: walker{at}mrc-dunn.cam.ac.uk


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