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Titolo:
Mammalian subunit IV isoforms of cytochrome c oxidase
Autore:
Huttemann, M; Kadenbach, B; Grossman, LI;
Indirizzi:
Wayne State Univ, Sch Med, Ctr Mol Med & Genet, Detroit, MI 48201 USA Wayne State Univ Detroit MI USA 48201 Med & Genet, Detroit, MI 48201 USA Univ Marburg, Fachbereich Chem, D-35032 Marburg, Germany Univ Marburg Marburg Germany D-35032 eich Chem, D-35032 Marburg, Germany
Titolo Testata:
GENE
fascicolo: 1, volume: 267, anno: 2001,
pagine: 111 - 123
SICI:
0378-1119(20010404)267:1<111:MSIIOC>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSCRIPTION FACTORS; NUCLEOTIDE-SEQUENCE; SKELETAL-MUSCLE; COMPLEX-III; SWISS-MODEL; MOUSE CDNA; RAT-LIVER; BINDING; GENES; MITOCHONDRIA;
Keywords:
cDNA; human; rat; mouse; oxygen; lung; in situ;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
42
Recensione:
Indirizzi per estratti:
Indirizzo: Grossman, LI Wayne State Univ, Sch Med, Ctr Mol Med & Genet, 540 E Canfield Ave, Detroit, MI 48201 USA Wayne State Univ 540 E Canfield Ave Detroit MIUSA 48201 USA
Citazione:
M. Huttemann et al., "Mammalian subunit IV isoforms of cytochrome c oxidase", GENE, 267(1), 2001, pp. 111-123

Abstract

Cytochrome c oxidase (COX) contains ten nuclear encoded subunits, three ofthem known to show tissue isoforms in mammals. We have now found a fourth isoform, for subunit IV, in human, rat and mouse (COX IV-2). Comparison of the two human isoform genes shows a similar structural organization, including an overall size of about 8 kb, the presence of five exons, and the initiation of translation in the second exon, consistent with formation by geneduplication. Also consistent is the higher identity of precursor peptides of 78% within the new IV-2 isoform (average in the three species) compared to 44% average identity with the IV-1 isoform. Northern analysis and quantitative PCR with human and rat tissues show high IV-2 expression in adult lung and lower expression in all other tissues investigated, including fetal lung. In contrast, the IV-1 isoform is ubiquitously expressed. In situ hybridizations were performed to localize isoform transcripts in rat lung. Bothisoforms are found in similar ratios in most lung cell types except for smooth muscle and respiratory epithelium, which have a IV-2 and a IV-1 preference, respectively. Structural modeling of the IV-2 isoform from human, based on the bovine crystal data, produces a conformation in which two of three conserved cysteine groups, exclusively present in the mammalian IV-2 isoform, are in close proximity. The formation of a cysteine bond and the implications for function of these sequence differences for subunit IV, which plays a pivotal role in COX regulation, are discussed. (C) 2001 Elsevier Science B.V. All rights reserved.

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Documento generato il 02/04/20 alle ore 02:35:09