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http://purl.uniprot.org/citations/17937768http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17937768http://www.w3.org/2000/01/rdf-schema#comment"Subunit 4 of cytochrome c oxidase (CcO) is a nuclear-encoded regulatory subunit of the terminal complex of the mitochondrial electron transport chain. We have recently discovered an isoform of CcO 4 (CcO4-2) which is specific to lung and trachea, and is induced after birth. The role of CcO as the major cellular oxygen consumer, and the lung-specific expression of CcO4-2, led us to investigate CcO4-2 gene regulation. We cloned the CcO4-2 promoter regions of cow, rat and mouse and compared them with the human promoter. Promoter activity is localized within a 118-bp proximal region of the human promoter and is stimulated by hypoxia, reaching a maximum (threefold) under 4% oxygen compared with normoxia. CcO4-2 oxygen responsiveness was assigned by mutagenesis to a novel promoter element (5'-GGACGTTCCCACG-3') that lies within a 24-bp region that is 79% conserved in all four species. This element is able to bind protein, and competition experiments revealed that, within the element, the four core bases 5'-TCNCA-3' are obligatory for transcription factor binding. CcO isolated from lung showed a 2.5-fold increased maximal turnover compared with liver CcO. We propose that CcO4-2 expression in highly oxygenated lung and trachea protects these tissues from oxidative damage by accelerating the last step in the electron transport chain, leading to a decrease in available electrons for free radical formation."xsd:string
http://purl.uniprot.org/citations/17937768http://purl.org/dc/terms/identifier"doi:10.1111/j.1742-4658.2007.06093.x"xsd:string
http://purl.uniprot.org/citations/17937768http://purl.uniprot.org/core/author"Liu J."xsd:string
http://purl.uniprot.org/citations/17937768http://purl.uniprot.org/core/author"Lee I."xsd:string
http://purl.uniprot.org/citations/17937768http://purl.uniprot.org/core/author"Grossman L.I."xsd:string
http://purl.uniprot.org/citations/17937768http://purl.uniprot.org/core/author"Huttemann M."xsd:string
http://purl.uniprot.org/citations/17937768http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17937768http://purl.uniprot.org/core/name"FEBS J"xsd:string
http://purl.uniprot.org/citations/17937768http://purl.uniprot.org/core/pages"5737-5748"xsd:string
http://purl.uniprot.org/citations/17937768http://purl.uniprot.org/core/title"Transcription of mammalian cytochrome c oxidase subunit IV-2 is controlled by a novel conserved oxygen responsive element."xsd:string
http://purl.uniprot.org/citations/17937768http://purl.uniprot.org/core/volume"274"xsd:string
http://purl.uniprot.org/citations/17937768http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17937768
http://purl.uniprot.org/citations/17937768http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/17937768
http://purl.uniprot.org/uniprot/#_H6SG14-mappedCitation-17937768http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17937768
http://purl.uniprot.org/uniprot/#_Q96KJ9-mappedCitation-17937768http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/17937768
http://purl.uniprot.org/uniprot/Q96KJ9http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/17937768
http://purl.uniprot.org/uniprot/H6SG14http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/17937768