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

被引:11
作者
Duborjal, H
Dupuis, A
Chapel, A
Kieffer, S
Lunardi, J
Issartel, JP
机构
[1] CEA GRENOBLE,DBMS,EA UJF 2019,LAB BIOENERGET CELLULAIRE & PATHOL,F-38054 GRENOBLE 9,FRANCE
[2] CEA GRENOBLE,DBMS,LAB CHIM PROTEMES,F-38054 GRENOBLE,FRANCE
关键词
Rhodobacter capsulatus; complex I; mitochondrion; gene sequence; immunopurification; MALDI mass spectrometry;
D O I
10.1016/S0014-5793(97)00212-3
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
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 immune-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. (C) 1997 Federation of European Biochemical Societies.
引用
收藏
页码:345 / 350
页数:6
相关论文
共 23 条
[1]  
ADESSI C, 1995, J CELL SCI, V108, P3331
[2]   SIMPLICITY AND COMPLEXITY IN ELECTRON-TRANSFER BETWEEN NADH AND C-TYPE CYTOCHROMES IN BACTERIA [J].
BERKS, BC ;
FERGUSON, SJ .
BIOCHEMICAL SOCIETY TRANSACTIONS, 1991, 19 (03) :581-588
[3]  
CHEN S, 1981, J BIOL CHEM, V256, P8318
[4]   IDENTIFICATION OF 2 GENES OF RHODOBACTER-CAPSULATUS CODING FOR PROTEINS HOMOLOGOUS TO THE ND1 AND 23 KDA SUBUNITS OF THE MITOCHONDRIAL COMPLEX-I [J].
DUPUIS, A .
FEBS LETTERS, 1992, 301 (02) :215-218
[5]   Identification of five Rhodobacter capsulatus genes encoding the equivalent of ND subunits of the mitochondrial NADH-ubiquinone oxidoreductase [J].
Dupuis, A ;
Peinnequin, A ;
Chevallet, M ;
Lunardi, J ;
Darrouzet, E ;
Pierrard, B ;
Procaccio, V ;
Issartel, JP .
GENE, 1995, 167 (1-2) :99-104
[6]   CONSERVATION OF SEQUENCES OF SUBUNITS OF MITOCHONDRIAL COMPLEX-I AND THEIR RELATIONSHIPS WITH OTHER PROTEINS [J].
FEARNLEY, IM ;
WALKER, JE .
BIOCHIMICA ET BIOPHYSICA ACTA, 1992, 1140 (02) :105-134
[7]   THE PROTON-PUMPING RESPIRATORY COMPLEX-I OF BACTERIA AND MITOCHONDRIA AND ITS HOMOLOG IN CHLOROPLASTS [J].
FRIEDRICH, T ;
STEINMULLER, K ;
WEISS, H .
FEBS LETTERS, 1995, 367 (02) :107-111
[8]   PURIFICATION AND MOLECULAR AND ENZYMIC PROPERTIES OF MITOCHONDRIAL NADH DEHYDROGENASE [J].
GALANTE, YM ;
HATEFI, Y .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1979, 192 (02) :559-568
[9]   IMMUNOCHEMICAL IDENTIFICATION OF A 2-SUBUNIT NADH-UBIQUINONE OXIDOREDUCTASE FROM PARACOCCUS-DENITRIFICANS [J].
GEORGE, CL ;
FERGUSON, SJ .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1984, 143 (03) :567-573
[10]   STRUCTURAL RELATIONSHIPS BETWEEN THE NADH DEHYDROGENASES OF PARACOCCUS-DENITRIFICANS AND BOVINE HEART-MITOCHONDRIA AS REVEALED BY IMMUNOLOGICAL CROSS-REACTIVITIES [J].
GEORGE, CL ;
FERGUSON, SJ ;
CLEETER, MWJ ;
RAGAN, CI .
FEBS LETTERS, 1986, 198 (01) :135-139