The Identification of Apocytochrome b as a Mitochondrial Gene Product and Immunological Evidence for Altered Apocytochrome b in Yeast Strains having Mutations in the COB Region of Mitochondrial DNA

Kreike, Jan; Bechmann, Helga; Hemert, Formijn J. van; Schweyen, Rudolf J.; Boer, Poppo H.; Kaudewitz, F.; Groot, G.S.P.

doi:10.1111/j.1432-1033.1979.tb19755.x

Cited by 50 publications

(9 citation statements)

References 31 publications

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“…The gene products annotated to function terms with the contributes_to qualifier should also be annotated to the complex term in the Cellular Component that has that molecular function. For example, the subunits of the S. cerevisiae mitochondrial respiratory chain complex III are all annotated to the Molecular Function term ‘ubiquinol-cytochrome-c reductase activity’ [GO:0008121] with the contributes_to qualifier (26) and to the complex term ‘mitochondrial respiratory chain complex III’ [GO:0005750] in the Cellular Component ontology. This qualifier is not used with terms in Biological Process ontology because biological processes are a collection of molecular events and by default gene products contribute to the whole process.…”

Section: Qualifiermentioning

confidence: 99%

A guide to best practices for Gene Ontology (GO) manual annotation

et al. 2013

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The Gene Ontology Consortium (GOC) is a community-based bioinformatics project that classifies gene product function through the use of structured controlled vocabularies. A fundamental application of the Gene Ontology (GO) is in the creation of gene product annotations, evidence-based associations between GO definitions and experimental or sequence-based analysis. Currently, the GOC disseminates 126 million annotations covering >374 000 species including all the kingdoms of life. This number includes two classes of GO annotations: those created manually by experienced biocurators reviewing the literature or by examination of biological data (1.1 million annotations covering 2226 species) and those generated computationally via automated methods. As manual annotations are often used to propagate functional predictions between related proteins within and between genomes, it is critical to provide accurate consistent manual annotations. Toward this goal, we present here the conventions defined by the GOC for the creation of manual annotation. This guide represents the best practices for manual annotation as established by the GOC project over the past 12 years. We hope this guide will encourage research communities to annotate gene products of their interest to enhance the corpus of GO annotations available to all.Database URL: http://www.geneontology.org

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Section: Qualifiermentioning

confidence: 99%

A guide to best practices for Gene Ontology (GO) manual annotation

et al. 2013

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“…The ERP spectra due to Rieske's iron-sulfur cluster were clearly shown when ascorbate was used as a reductant for wild- 4. EPR spectra of iron-sulfur clusters 9 1 and S-2 at 15K.…”

Section: Presence Of Subunit V (The Iron-sulfur Protein) In Mitochondmentioning

confidence: 99%

The presence of the iron‐sulfur protein (subunit V) of complex III in mitochondria of heme‐deficient yeast cells lacking iron‐sulfur clusters detectable by electron paramagnetic resonance

Lin

Ohnishi

Clejan

et al. 1983

European Journal of Biochemistry

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The presence of subunit V, the iron-sulfur protein, of complex 111 has been demonstrated in mitochondria from a mutant of Saccharomyces cerevisiae which lacks 5-aminolevulinic acid synthase and, hence, is devoid of heme. The mature form (24 kDa) of the iron-sulfur protein was observed in equal amounts in the heme-deficient and hemesufficient cells with antiserum against subunit V and either the sensitive immuno-transfer technique or immunoprecipitation from dodecylsulfate-solubilized mitochondria. In addition, a slight shoulder with a molecular mass 1.5 kDa larger than the mature form was present in mitochondria from the heme-deficient cells.Electron paramagnetic resonance spectroscopy revealed the absence of iron-sulfur signals due to clusters S-I, S-2 and S-3 of succinate dehydrogenase o r to Rieske's iron-sulfur cluster of complex 111 in mitochondria from the hemedeficient cells. The lack of iron-sulfur centers in these cells may be a consequence of the absence of sulfite reductase in the cells without heme.Complex 111 of the mitochondrial respiratory chain catalyzes electron transport, coupled to ATP synthesis and ion transport, from ubiquinone to cytochrome c. Purified complex I11 from yeast mitochondria contains at least seven subunits with molecular masses ranging over 50-15.5 kDa [I]. Of the different subunits of the complex, only cytochrome b has been shown to be a mitochondrial translation product [2-41; all other subunits are synthesized on cytoplasmic ribosomes and transferred into the mitochondria in a subsequent step [5, 61. The possible regulation of protein synthesis in both the mitochondria and the cytosol such that the enzyme complexes of the mitochondrial membrane are assembled in an orderly manner has been extensively studied [7,8]. Various factors such as heme [9] and cytoplasmic proteins [8] Subsequently, the presence of the two 'core' proteins, apocytochrome b and the iron-sulfur protein, was observed in mitochondria from the heme-deficient cells [12]. By contrast, the mature form of cytochrome c1 does not appear in the mitochondrial membrane of heme-deficient cells [13]. Instead, an intermediate-sized form of the protein derived from the precursor synthesized in the cytoplasm accumulates [131. TheAbbreviations. SDS, sodium dodecyl sulfate; ERP, electron paramagnetic resonance; Hipip, high-potential iron-sulfur protein.assembly of cytochrome oxidase is also regulated by heme in a complicated manner [14].In the present study, the presence of equivalent amounts of the mature form of the iron-sulfur protein of complex I11 has been demonstrated in heme-deficient and wild-type cells by immunoprecipitation of SDS-solubilized mitochondria from radiolabeled cells and subunit-specific antiserum [l]. Furthermore, a prominent shoulder with a molecular mass 1 -1.5 kDa larger than the mature form of the iron-sulfur protein was observed in the mitochondria from the heme-deficient cells but not in wild-type cells using the sensitive immuno-transfer technique. EPR spectra revealed the complete absence o...

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“…(c) Some mutants produced a smaller polypeptide, presumably by premature chain termination. Other mutants, interspersed with those of the first class, produced polypeptides up to twice the size of cytochrome b but which nonetheless cross-reacted with antibody to cytochrome b, suggesting that translation was now occurring in regions that were not normally translated (Haid et al, 1979;Kreike et al, 1979;. More direct evidence for the presence of introns in COB has been obtained by electron microscopy of DNA-RNA hybrids .…”

Section: Mosaic Genes In Yeast Mitochondriamentioning

confidence: 99%

“…Moreover, box-3, -7 and -10 mutants are pleiotropic, and block expression of the OXI3 gene. Thus, these mutations are recessive but affect some function that normally acts in trans on both the COB and OXI3 genes, one possibility of course being that the introns in the cytochrome b gene were needed for RNA splicing (Kreike et al, 1979;Church et al, 1979).…”

Section: Mosaic Genes In Yeast Mitochondriamentioning

confidence: 99%

The molecular biology of the mitochondrion

Rosamond¹

1982

Biochemical Journal

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The Identification of Apocytochrome b as a Mitochondrial Gene Product and Immunological Evidence for Altered Apocytochrome b in Yeast Strains having Mutations in the COB Region of Mitochondrial DNA

Cited by 50 publications

References 31 publications

A guide to best practices for Gene Ontology (GO) manual annotation

A guide to best practices for Gene Ontology (GO) manual annotation

The presence of the iron‐sulfur protein (subunit V) of complex III in mitochondria of heme‐deficient yeast cells lacking iron‐sulfur clusters detectable by electron paramagnetic resonance

The molecular biology of the mitochondrion

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