Immuno‐purification of a dimeric subcomplex of the respiratory NAHD‐CoQ reductase of Rhodobacter capsulatus equivalent to the FP fraction of the mitochondrial complex I

FEBS Letters

Lunardi, Joël¹  Kieffer, Silvie²  Chapel, Agnès²  Duborjal, Hervé¹  Dupuis, Alain¹  Issartel, Jean-Paul¹ 

[1] Laboratoire de Bioénergétique Cellulaire et Pathologique, EA 2019 UJF, DBMS, CEA Grenoble, 38054 Grenoble Cedex 9, France;Laboratoire de Chimie des Protéines, DBMS, CEA Grenoble, 38054 Grenoble Cedex 9, France

关键词: Rhodobacter capsulatus;    Complex I;    Mitochondrion;    Gene sequence;    Immunopurification;    MALDI mass spectrometry;    NUO;    NADH-ubiquinone oxidoreductase;    FP;    flavoprotein fraction;    MALDI;    matrix-assisted laser desorption/ionization;    PNE;    synthetic peptide corresponding to the NUOE subunit N-terminus;   

DOI  :  10.1016/S0014-5793(97)00212-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The Rhodobacter capsulatus genes encoding the NUOE and NUOF subunits, equivalent to the 24 kDa and 51 kDa subunits of the mammalian mitochondrial complex I, have been sequenced. According to the nucleotide sequence, the NUOE subunit is 389 amino acids long and has a molecular mass of 41.3 kDa. In comparison to the mitochondrial equivalent subunit, NUOE is extended at the C terminus by more than 150 amino acids. The NUOF subunit is 431 amino acids long and has a molecular mass of 47.1 kDa. A subcomplex containing both the NUOE and NUOF subunits was extracted by detergent treatment of R. capsulatus membranes and immuno-purified. This subcomplex is homologous to the mitochondrial FP fragment. Mass spectrometry after trypsin treatment of the NUOE subunit validates the atypical primary structure deduced from the sequence of the gene.

【 授权许可】

Unknown