Amino Acid Replacement Studies of Human Cytochrome c by a Complementation System Using CYC1 Deficient Yeast
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 replace...
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| Veröffentlicht in: | Journal of biochemistry (Tokyo) 1988-09, Vol.104 (3), p.477-480 |
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| container_title | Journal of biochemistry (Tokyo) |
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| creator | Tanaka, Yoshikazu Ashikari, Toshihiko Shibano, Yuji Amachi, Teruo Yoshizumi, Hajime Matsubara, Hiroshi |
| description | 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. Cytochromec 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. |
| doi_str_mv | 10.1093/oxfordjournals.jbchem.a122493 |
| format | Article |
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Invariant Cys-17 and Arg-38 could not be replaced by alanine and tryptophan, respectively, without function impairment. Cytochromec 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.</description><identifier>ISSN: 0021-924X</identifier><identifier>EISSN: 1756-2651</identifier><identifier>DOI: 10.1093/oxfordjournals.jbchem.a122493</identifier><identifier>PMID: 2853705</identifier><identifier>CODEN: JOBIAO</identifier><language>eng</language><publisher>Oxford: Oxford University Press</publisher><subject>amino acids ; Amino Acids - analysis ; Analytical, structural and metabolic biochemistry ; Base Sequence ; Biological and medical sciences ; cytochrome c ; Cytochrome c Group - genetics ; DNA, Recombinant ; Fundamental and applied biological sciences. Psychology ; genes ; Genetic Complementation Test ; Hemoproteins ; Humans ; Metalloproteins ; Molecular Sequence Data ; Mutation ; Proteins ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - genetics</subject><ispartof>Journal of biochemistry (Tokyo), 1988-09, Vol.104 (3), p.477-480</ispartof><rights>1989 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c491t-dedd5245a149f1ed78e754428177a2ba01a10896a22b95b42aaf628475bd0cf83</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7124581$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2853705$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tanaka, Yoshikazu</creatorcontrib><creatorcontrib>Ashikari, Toshihiko</creatorcontrib><creatorcontrib>Shibano, Yuji</creatorcontrib><creatorcontrib>Amachi, Teruo</creatorcontrib><creatorcontrib>Yoshizumi, Hajime</creatorcontrib><creatorcontrib>Matsubara, Hiroshi</creatorcontrib><title>Amino Acid Replacement Studies of Human Cytochrome c by a Complementation System Using CYC1 Deficient Yeast</title><title>Journal of biochemistry (Tokyo)</title><addtitle>J Biochem</addtitle><description>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. Cytochromec 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.</description><subject>amino acids</subject><subject>Amino Acids - analysis</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>cytochrome c</subject><subject>Cytochrome c Group - genetics</subject><subject>DNA, Recombinant</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>genes</subject><subject>Genetic Complementation Test</subject><subject>Hemoproteins</subject><subject>Humans</subject><subject>Metalloproteins</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>Proteins</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - genetics</subject><issn>0021-924X</issn><issn>1756-2651</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1988</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1v1DAQhi0EKtvCT0DyAbhl8WdsHzisUugirYSgFFouluM41Ns4XuxE6v57smy0EidOI-t9ZsaaB4A3GC0xUvRdfGxjarZxTL3p8nJb23sXlgYTwhR9AhZY8LIgJcdPwQIhggtF2O1zcJ7z9vAklJ6BMyI5FYgvwMMq-D7ClfUN_Op2nbEuuH6A18PYeJdhbOF6DKaH1X6I9j7F4KCF9R4aWMWw6_7SZvCxh9f7PLgAb7Lvf8HqrsLw0rXe-sO4O2fy8AI8a6cvu5dzvQA3Hz98q9bF5vPVp2q1KSxTeCga1zScMG4wUy12jZBOcMaIxEIYUhuEDUZSlYaQWvGaEWPakkgmeN0g20p6Ad4e5-5S_D26POjgs3VdZ3oXx6yFFIQySf8LYo5RKUs1ge-PoE0x5-RavUs-mLTXGOmDFf2vFX20omcrU_-redFYB9ecumcNU_56zk22pmuT6a3PJ0zg6RwST1hxxPx06cdTbNKDLgUVXK9vf-of6LtSavNFE_oHxuysNQ</recordid><startdate>19880901</startdate><enddate>19880901</enddate><creator>Tanaka, Yoshikazu</creator><creator>Ashikari, Toshihiko</creator><creator>Shibano, Yuji</creator><creator>Amachi, Teruo</creator><creator>Yoshizumi, Hajime</creator><creator>Matsubara, Hiroshi</creator><general>Oxford University Press</general><scope>BSCLL</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M7N</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19880901</creationdate><title>Amino Acid Replacement Studies of Human Cytochrome c by a Complementation System Using CYC1 Deficient Yeast</title><author>Tanaka, Yoshikazu ; Ashikari, Toshihiko ; Shibano, Yuji ; Amachi, Teruo ; Yoshizumi, Hajime ; Matsubara, Hiroshi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c491t-dedd5245a149f1ed78e754428177a2ba01a10896a22b95b42aaf628475bd0cf83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1988</creationdate><topic>amino acids</topic><topic>Amino Acids - analysis</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>cytochrome c</topic><topic>Cytochrome c Group - genetics</topic><topic>DNA, Recombinant</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>genes</topic><topic>Genetic Complementation Test</topic><topic>Hemoproteins</topic><topic>Humans</topic><topic>Metalloproteins</topic><topic>Molecular Sequence Data</topic><topic>Mutation</topic><topic>Proteins</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Tanaka, Yoshikazu</creatorcontrib><creatorcontrib>Ashikari, Toshihiko</creatorcontrib><creatorcontrib>Shibano, Yuji</creatorcontrib><creatorcontrib>Amachi, Teruo</creatorcontrib><creatorcontrib>Yoshizumi, Hajime</creatorcontrib><creatorcontrib>Matsubara, Hiroshi</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of biochemistry (Tokyo)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tanaka, Yoshikazu</au><au>Ashikari, Toshihiko</au><au>Shibano, Yuji</au><au>Amachi, Teruo</au><au>Yoshizumi, Hajime</au><au>Matsubara, Hiroshi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Amino Acid Replacement Studies of Human Cytochrome c by a Complementation System Using CYC1 Deficient Yeast</atitle><jtitle>Journal of biochemistry (Tokyo)</jtitle><addtitle>J Biochem</addtitle><date>1988-09-01</date><risdate>1988</risdate><volume>104</volume><issue>3</issue><spage>477</spage><epage>480</epage><pages>477-480</pages><issn>0021-924X</issn><eissn>1756-2651</eissn><coden>JOBIAO</coden><abstract>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. Cytochromec 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.</abstract><cop>Oxford</cop><pub>Oxford University Press</pub><pmid>2853705</pmid><doi>10.1093/oxfordjournals.jbchem.a122493</doi><tpages>4</tpages></addata></record> |
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| subjects | amino acids Amino Acids - analysis Analytical, structural and metabolic biochemistry Base Sequence Biological and medical sciences cytochrome c Cytochrome c Group - genetics DNA, Recombinant Fundamental and applied biological sciences. Psychology genes Genetic Complementation Test Hemoproteins Humans Metalloproteins Molecular Sequence Data Mutation Proteins Saccharomyces cerevisiae Saccharomyces cerevisiae - genetics |
| title | Amino Acid Replacement Studies of Human Cytochrome c by a Complementation System Using CYC1 Deficient Yeast |
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