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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
1991-7-19
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pubmed:abstractText |
Genes coding for polyproteins that are cleaved posttranslationally into two or more functional proteins are rarely found in prokaryotes. One example concerns the biogenesis of the Bradyrhizobium japonicum cytochromes b and c1, two of the three constituent subunits of ubiquinol-cytochrome-c reductase (ubiquinol:ferricytochrome-c oxidoreductase, EC 1.10.2.2); the respective apoproteins for these subunits are encoded by the 5' and 3' halves of a single gene, fbcH. These two halves are linked by an extra piece of DNA encoding a characteristic signal peptide for protein translocation across the cytoplasmic membrane. Processing of the fbcH gene product is shown to occur at a typical signal peptidase recognition site. This reaction is reminiscent of that catalyzed by the regular bacterial signal peptidase that normally cleaves off presequences from the N termini of translocated proteins. Mutational alteration of the signal peptidase recognition site within FbcH results in the appearance of an uncleaved bc1 fusion protein in the membrane. Additionally, a functional heme-binding site in the apocytochrome c1 section of FbcH is shown to be a necessary prerequisite for the formation of the bc1 complex.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647023-1965217,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647023-2163487,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647023-2172221,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647023-2172694,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647023-2188944,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647023-2205499,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647023-2281528,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647023-232214,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647023-2406905,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647023-2464578,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647023-2470367,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647023-2536325,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647023-2541921,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647023-2542325,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647023-2548064,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647023-2646712,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647023-2982819,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647023-3001650,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647023-3004982,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647023-3032252,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647023-3052288,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647023-3542570,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647023-3552675,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647023-3611052,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647023-377280,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647023-3949810,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647023-6293932,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647023-6310323,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647023-6383203,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647023-6639271,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647023-6697395,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647023-6852022,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647023-6855576,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647023-7012838
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
88
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5001-5
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:1647023-Amino Acid Sequence,
pubmed-meshheading:1647023-Base Sequence,
pubmed-meshheading:1647023-Binding Sites,
pubmed-meshheading:1647023-Chromosomes, Bacterial,
pubmed-meshheading:1647023-Cytochrome b Group,
pubmed-meshheading:1647023-Cytochromes c1,
pubmed-meshheading:1647023-Endopeptidases,
pubmed-meshheading:1647023-Genes, Bacterial,
pubmed-meshheading:1647023-Genetic Complementation Test,
pubmed-meshheading:1647023-Heme,
pubmed-meshheading:1647023-Membrane Proteins,
pubmed-meshheading:1647023-Molecular Sequence Data,
pubmed-meshheading:1647023-Mutagenesis, Site-Directed,
pubmed-meshheading:1647023-Oligonucleotide Probes,
pubmed-meshheading:1647023-Protein Processing, Post-Translational,
pubmed-meshheading:1647023-Rhizobiaceae,
pubmed-meshheading:1647023-Serine Endopeptidases
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pubmed:year |
1991
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pubmed:articleTitle |
From one gene to two proteins: the biogenesis of cytochromes b and c1 in Bradyrhizobium japonicum.
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pubmed:affiliation |
Mikrobiologisches Institut, Eidgenössische Technische Hochschule, ETH-Zentrum, Zürich, Switzerland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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