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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
1989-5-19
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pubmed:abstractText |
Various in vitro mutated human cytochrome c genes which encode displaced amino acid residues at the 14th, 17th, 28th, 37th, 38th, 56th, and/or 84th residues were constructed, and their degrees of complementation of yeast CYC1 deficiency were examined. Invariant Cys-17 and Arg-38 could not be replaced by alanine and tryptophan, respectively, without function impairment. Cytochrome c containing Ala-14 instead of conserved Cys-14, Gly-38 or Lys-38 instead of Arg-38, and Ser-84 instead of invariant Gly-84 were partly functional. These results indicate that these invariant or conserved residues are important. Cytochromes c containing Cys-56 instead of native Gly-56 was partly functional. Cytochrome c containing Arg-37 and Gly-38 instead of Gly-37 and Arg-38 was slightly functional. Replacement of variable Thr-28 and Gly-37 by Ile-28 and Arg-37, respectively, produced no effects. Our results are as a whole consistent with the view that conserved residues are important and variable residues are less important for cytochrome c to function.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-924X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
104
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
477-80
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pubmed:dateRevised |
2007-12-19
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pubmed:meshHeading |
pubmed-meshheading:2853705-Amino Acids,
pubmed-meshheading:2853705-Base Sequence,
pubmed-meshheading:2853705-Cytochrome c Group,
pubmed-meshheading:2853705-DNA, Recombinant,
pubmed-meshheading:2853705-Genetic Complementation Test,
pubmed-meshheading:2853705-Humans,
pubmed-meshheading:2853705-Molecular Sequence Data,
pubmed-meshheading:2853705-Mutation,
pubmed-meshheading:2853705-Saccharomyces cerevisiae
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pubmed:year |
1988
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pubmed:articleTitle |
Amino acid replacement studies of human cytochrome c by a complementation system using CYC1 deficient yeast.
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pubmed:affiliation |
Institute for Fundamental Research, Research Center, Suntory Ltd., Osaka.
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pubmed:publicationType |
Journal Article
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