Characterization of two different genes (cDNA) for cytochrome c oxidase subunit VIa from heart and liver of the rat.

Schlerf, Andrea; Droste, M.; Winter, Matthew J.; Kadenbach, Bernhard

doi:10.1002/j.1460-2075.1988.tb03083.x

Cited by 116 publications

(53 citation statements)

References 31 publications

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“…(B cyt45011); rat ornithine carbamoyltransferase [36], (R oct); human pyruvate dehydrogenase EI~ subunit [37], (H PyrDhE1); bovine mitochondrial adenylate kinase 2 [38], (B AK2A, B AK2B); bovine mitochondrial carrier protein [39], (B mtPcP); rat mitochondrial 3-oxoacyl-CoA thiolase [40], (R 3oxCoth); human liver glutamate dehydrogenase [41], (H GDH); rat heart and liver subunit Via of cytochrome oxidase [42], (R hcoxVIa. R IcoxVla); mouse mitochondrial uncoupling protein [43], (M Ucp, M Ucp/min); mouse ornithine transcarbamylase [44], (Motc); mouse mitochondrial malate dehydrogenase [45], (M mMDH); human cytochrome oxidase subunit Vie [46], (H coxVIc); human aspartate amino transferase [47], (H mAspAT); rat liver mitochondrial NADH dehydrogenase 24-kDa subunit [67], (H cox-VIII); murine NAD-dependent methylenetetrahydrofolate dehydrogenase-melthylenyltetrahydrofolate cyclohydrolase [68], (M MTHFdeh); bovine GTP:AMP phosphotransferase [69], (B AK3); bovine NADH-ubiquinone reductase [70], (B ubiqred); human methylmalonyl-CoA mutase [71], (H Metmlmt); human mitochondrial protein homologous to the bacterial and plant chaperonms [72], (H PI); porcine testis cytochrome P-450 (SCC) [73], (P cytp450); human cytochrome oxidase subunit Vlb [74], (H coxVIb); human creatine kinase [7'5].…”

Section: Resultsmentioning

confidence: 99%

Analysis of the polyadenylation consensus sequence context in the genes of nuclear encoded mitochondrial proteins

Juretić

Theus

1991

FEBS Letters

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A compilation of the pre-mRNA ends of the genes of nuclear encoded mitochondrial proteins resulted in a consensus sequence of the type (T/A)NTTNNNNNTTTNAATAAA. Nucleotide positions +8, +13. +14, +16 and +17 downstream of the AATAAA sequence show also a predominance of nucleotide T. This consensus sequence suggests the importance of the immediate surroundings of the cannonical polyadenylation signal sequence AATAAA on the efficiency of" the cleavage and polyadenylation of this specific group of pre-mRNAs.Nuclear encoded mitochondrial protein; RNA processing

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Section: Resultsmentioning

confidence: 99%

Analysis of the polyadenylation consensus sequence context in the genes of nuclear encoded mitochondrial proteins

Juretić

Theus

1991

FEBS Letters

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“…Among these proteins are the adenine nucleotide carrier (45)(46)(47)(48), the uncoupling protein (49,50), the human ␥-subunit of the ATP synthase complex (51), the mammalian proteolipid subunit of ATP synthase (52), and the three mammalian subunits (VIa, VIIa, and VIII) of cytochrome oxidase (53,54). The common feature of all these proteins is the presence of at least one heart type isoform, which is abundantly expressed only in muscles, and one liver type isoform, which is ubiquitously expressed in all tissues.…”

Section: Constants Of Recombinant Pic-a and Pic-b Isoformsmentioning

confidence: 99%

Expression in Escherichia coli, Functional Characterization, and Tissue Distribution of Isoforms A and B of the Phosphate Carrier from Bovine Mitochondria

Fiermonte¹,

Dolce²,

Palmieri

1998

Journal of Biological Chemistry

136

125

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The two isoforms of the mammalian mitochondrial phosphate carrier (PiC), A and B, differing in the sequence near the N terminus, arise from alternative splicing of a primary transcript of the PiC gene (Dolce, V., Iacobazzi, V., Palmieri, F., and Walker, J. E. (1994) J. Biol. Chem. 269, 10451-10460). To date, the PiC isoforms A and B have not been studied at the protein level. To explore the tissue-distribution and the potential functional differences between the two isoforms, polyclonal site-directed antibodies specific for PiC-A and PiC-B were raised, and the two bovine isoforms were obtained by expression in Escherichia coli and reconstituted into phospholipid vesicles. Western blot analysis demonstrated that isoform A is present in high amounts in heart, skeletal muscle, and diaphragm mitochondria, whereas isoform B is present in the mitochondria of all tissues examined. Heart and liver bovine mitochondria contained 69 and 0 pmol of PiC-A/mg of protein, and 10 and 8 pmol of PiC-B/mg of protein, respectively. In the reconstituted system the pure recombinant isoforms A and B both catalyzed the two known modes of transport (P i /P i antiport and P i /H ؉ symport) and exhibited similar properties of substrate specificity and inhibitor sensitivity. However, they strongly differed in their kinetic parameters. The transport affinities of isoform B for phosphate and arsenate were found to be 3-fold lower than those of isoform A. Furthermore, the maximum transport rate of isoform B is about 3-fold higher than that of isoform A. These results support the hypothesis that the sequence divergence between PiC-A and PiC-B may have functional significance in determining the affinity and the translocation rate of the substrate through the PiC molecule.The transport of inorganic phosphate across the inner mitochondrial membrane into the matrix compartment is essential for the oxidative phosphorylation of ADP to ATP. This transport is catalyzed by the phosphate carrier (PiC) 1 which has been purified from different sources and reconstituted into liposomes in an active form (1-4). In the reconstituted system the native bovine PiC protein catalyzes the P i /H ϩ symport as well as the P i /P i exchange, which functions by a sequential mechanism (5). The primary structure of the mature PiC is made up of three tandemly related domains about 100 amino acids in length (6). These repetitive elements are related to those found in the other well characterized members of the mitochondrial carrier family (see Refs. 7-10 for reviews) (11,12). They are also found in a number of other proteins of known sequence but of unknown function, which therefore belong to the same protein superfamily (7-10). By examination of the transmembrane topography of the PiC in the inner mitochondrial membrane, it has been proposed that both the N-and C-terminal regions of the PiC protrude toward the cytosol and that the polypeptide chain spans the membrane six times (13). Only one gene for the PiC has been detected in man and cow (14), of which the human one has...

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“…Blots were prehybridized for 1 h at 65 "C in 0.125 M sodium phosphate pH 7.2, 0.25 M NaCl, 1.25 mM EDTA, 7% SDS, 1 % bovine serum albumin, 10% poly(ethy1ene glycol) (Ma 4000-6000). After an overnight hybridization with labelled DNA probes at 65 "C, the filters were washed twice for 10 min in 2X NaCl/Cit, 0.1 % Blots with total cellular RNA (4 pg) from liver (L), skeletal muscle (S), heart (H) and intestine (I) were hybridized with DNA probes for the different subunits of COX (I,11, 111, IV, Va, Vb, VIaL, VIaH, VIb, VIc, VIIaL, VIIaH, VIIb, VIIc, and VIII), as well as an oligonucleotide probe for the human 28s rRNA to check for possible unequal loading. SDS at room temperature, then 15 min at 65 "C in 1 X NaCI/ Cit, 0.1% SDS, and finally twice for 10 min at 65°C in 0.1 X NaClICit, 0.1 % SDS.…”

Section: Rna Isolation and Northern Blot Analysismentioning

confidence: 99%

Expression of human cytochrome c, oxidase subunits during fetal development

Bonne

Seibel²,

Possekel

et al. 1993

European Journal of Biochemistry

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Expression of human cytochrome c oxidase (COX) subunits was examined at fetal (20-28 weeks) and adult state by Northern blot hybridization with mRNA from liver, heart, skeletal muscle, and intestine. The data were related to COX and citrate synthase activities and to immunodetected COX subunits (II/III, IV, VIIaH). In liver little changes of COX transcripts are observed from fetal to adult state. In contrast, in heart and skeletal muscle all transcripts of COX subunits increase between 2-20-fold, when related to the amount of 28s rRNA. In fetal heart and skeletal muscle the relative amounts of the liver-type transcripts of subunit VIa were 30% and 25% from total VIa transcripts (VIaL + VIaH), respectively, but decrease to only 2-5% at adult state. The liver-type transcripts of subunit VIIa occur to 50% in fetal heart and skeletal muscle, which remained unchanged in adult heart and decrease to 5 8 % in adult skeletal muscle. The results clearly indicate a switch of gene expression in heart and skeletal muscle during development, from the liver type to the headmuscle type of subunit VIa (and partly VIIa).Cytochrome c oxidase (COX) is the terminal enzyme complex of the respiratory chain, coupling the transfer of electrons from cytochrome c to molecular oxygen with the concomitant production of a proton electrochemical gradient across the inner mitochondrial membrane [l]. In mammals, the enzyme consists of 13 dissimilar polypeptides [ 2 ] . The three largest subunits (1-111) are encoded by the mitochondrial genome and constitute the catalytic core of the enzyme [3, 41. The ten smaller nuclear gene products [S] have been suggested to play a keyrole in the regulation of the enzyme [6, 71. Recently it was demonstrated [8, 91 that the activity and energy transduction of COX from heart and skeletal muscle is tissue-specific and regulated by nucleotides via interaction with subunit VIaH (heart/muscle type).The mammalian COX occurs in tissue-specific isoforms differing in the isotype of subunits VIa, VIIa and/or VIII (liver type or heart/muscle type). This has been demonstrated by immunological, electrophoretic and amino acid sequence differences between corresponding nuclear-coded subunits of COX from different mammalian tissues and species [2, 5, 101. These findings have been confirmed by cloning and sequencing of cDNAs coding for the different subunits of tissue-specific isoforms for subunit VIa of rat [ I l l , VIIa [lo,12, 161 and VIII [lo, 131 occur as liver (L) and heart (H) isoforms. In rat only the L form of subunit VIIa was found [17, 181, but both isoforms of subunits VIa [ l l ] and VIII [19]. In human, subunit VIII is present only in the L form [20, 211, whereas both isoforms occur for subunits VIa [22, Most of the other nuclearcoded subunits have been cloned and sequenced from rat, beef and human (for review see [28, 291).A co-ordinate expression of the mitochondrial-coded subunit 111 and the nuclear-coded subunit VIc has been demonstrated in rat tissues under steady-state conditions [30-321. Under non-s...

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Characterization of two different genes (cDNA) for cytochrome c oxidase subunit VIa from heart and liver of the rat.

Cited by 116 publications

References 31 publications

Analysis of the polyadenylation consensus sequence context in the genes of nuclear encoded mitochondrial proteins

Analysis of the polyadenylation consensus sequence context in the genes of nuclear encoded mitochondrial proteins

Expression in Escherichia coli, Functional Characterization, and Tissue Distribution of Isoforms A and B of the Phosphate Carrier from Bovine Mitochondria

Expression of human cytochrome c, oxidase subunits during fetal development

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