Source:http://linkedlifedata.com/resource/pubmed/id/10899162
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
39
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pubmed:dateCreated |
2000-10-27
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pubmed:databankReference | |
pubmed:abstractText |
The algae of the family Chlamydomonadaceae lack the gene cox3 that encodes subunit III of cytochrome c oxidase in their mitochondrial genomes. This observation has raised the question of whether this subunit is present in cytochrome c oxidase or whether the corresponding gene is located in the nucleus. Cytochrome c oxidase was isolated from the colorless chlamydomonad Polytomella spp., and the existence of subunit III was established by immunoblotting analysis with an antibody directed against Saccharomyces cerevisiae subunit III. Based partly upon the N-terminal sequence of this subunit, oligodeoxynucleotides were designed and used for polymerase chain reaction amplification, and the resulting product was used to screen a cDNA library of Chlamydomonas reinhardtii. The complete sequences of the cox3 cDNAs from Polytomella spp. and C. reinhardtii are reported. Evidence is provided that the genes for cox3 are encoded by nuclear DNA, and the predicted polypeptides exhibit diminished physical constraints for import as compared with mitochondrial-DNA encoded homologs. This indicates that transfer of this gene to the nucleus occurred before Polytomella diverged from the photosynthetic Chlamydomonas lineage and that this transfer may have occurred in all chlamydomonad algae.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/COX3 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Electron Transport Complex IV,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Sorting Signals,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
29
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pubmed:volume |
275
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
30144-52
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:10899162-Amino Acid Sequence,
pubmed-meshheading:10899162-Angiosperms,
pubmed-meshheading:10899162-Animals,
pubmed-meshheading:10899162-Cell Nucleus,
pubmed-meshheading:10899162-Chlorophyta,
pubmed-meshheading:10899162-Electron Transport Complex IV,
pubmed-meshheading:10899162-Eukaryota,
pubmed-meshheading:10899162-Membrane Proteins,
pubmed-meshheading:10899162-Mitochondria,
pubmed-meshheading:10899162-Molecular Sequence Data,
pubmed-meshheading:10899162-Phylogeny,
pubmed-meshheading:10899162-Polymerase Chain Reaction,
pubmed-meshheading:10899162-Protein Sorting Signals,
pubmed-meshheading:10899162-Protein Structure, Quaternary,
pubmed-meshheading:10899162-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:10899162-Sequence Analysis, DNA,
pubmed-meshheading:10899162-Sequence Homology, Amino Acid
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pubmed:year |
2000
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pubmed:articleTitle |
Unusual location of a mitochondrial gene. Subunit III of cytochrome C oxidase is encoded in the nucleus of Chlamydomonad algae.
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pubmed:affiliation |
Departamento de Genética Molecular, Instituto de Fisiologia Celular, Universidad Nacional Autónoma de México, 04510.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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