apg15-1, a UGA mutant allele in the Saccharomyces cerevisiae APG16 gene, and its suppression by a cytoplasmic factor
Autophagy is a complex cellular process by which starving cells utilize cytoplasmic macromolecules as nutritional resources. In Saccharomyces cerevisiaey more than 15 genes are involved in this process and most of them have been cloned and characterized by now. But there remains a complementation gr...
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| Veröffentlicht in: | Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2004-07, Vol.68 (7), p.1541-1548 |
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| creator | Okazaki, H. (Teikyo Univ. of Science and Technology, Uenohara, Yamanashi (Japan)) Ono, B Ohsumi, Y Ohsumi, M |
| description | Autophagy is a complex cellular process by which starving cells utilize cytoplasmic macromolecules as nutritional resources. In Saccharomyces cerevisiaey more than 15 genes are involved in this process and most of them have been cloned and characterized by now. But there remains a complementation group represented by a single mutation, apg15-1 , unclear as to its molecular nature. We obtained DNA fragments that functionally complemented apg15-1 and found that the responsible ORF, YMR159C, was already assigned as APG16. It was further found that apg15-1 was a UGA allele in which the 243rd base of the 450 bp coding region o(APG16 was converted from C to T, and that the previously observed complementation between apg15-1 and apg16D was attributable to the action of a cytoplasmic omnipotent suppressor. This suppressor was readily cured by guanidine-HCl and also by overexpression or disruption of HSP104, indicating its close similarity to the PSI prion-like factor. Since apg15-1 is a mutation highly sensitive to termination suppression, it can be used as a tool to detect weak termination suppressors. |
| doi_str_mv | 10.1271/bbb.68.1541 |
| format | Article |
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(Teikyo Univ. of Science and Technology, Uenohara, Yamanashi (Japan)) ; Ono, B ; Ohsumi, Y ; Ohsumi, M</creator><creatorcontrib>Okazaki, H. (Teikyo Univ. of Science and Technology, Uenohara, Yamanashi (Japan)) ; Ono, B ; Ohsumi, Y ; Ohsumi, M</creatorcontrib><description>Autophagy is a complex cellular process by which starving cells utilize cytoplasmic macromolecules as nutritional resources. In Saccharomyces cerevisiaey more than 15 genes are involved in this process and most of them have been cloned and characterized by now. But there remains a complementation group represented by a single mutation, apg15-1 , unclear as to its molecular nature. We obtained DNA fragments that functionally complemented apg15-1 and found that the responsible ORF, YMR159C, was already assigned as APG16. It was further found that apg15-1 was a UGA allele in which the 243rd base of the 450 bp coding region o(APG16 was converted from C to T, and that the previously observed complementation between apg15-1 and apg16D was attributable to the action of a cytoplasmic omnipotent suppressor. This suppressor was readily cured by guanidine-HCl and also by overexpression or disruption of HSP104, indicating its close similarity to the PSI prion-like factor. Since apg15-1 is a mutation highly sensitive to termination suppression, it can be used as a tool to detect weak termination suppressors.</description><identifier>ISSN: 0916-8451</identifier><identifier>EISSN: 1347-6947</identifier><identifier>DOI: 10.1271/bbb.68.1541</identifier><identifier>PMID: 15277759</identifier><language>eng</language><publisher>Tokyo: Japan Society for Bioscience, Biotechnology, and Agrochemistry</publisher><subject>Alleles ; Aminopeptidases - antagonists & inhibitors ; Aminopeptidases - physiology ; autophagy ; Autophagy - genetics ; Autophagy - physiology ; Autophagy-Related Proteins ; Biological and medical sciences ; Blotting, Western ; Carrier Proteins - antagonists & inhibitors ; Carrier Proteins - genetics ; Carrier Proteins - physiology ; Cloning, Molecular ; Cvt pathway ; CYTOPLASM ; CYTOSINE ; DNA, Bacterial - chemistry ; DNA, Bacterial - genetics ; EFFECTORS ; Fundamental and applied biological sciences. Psychology ; GENES ; Genetic Complementation Test ; Guanidine - pharmacology ; Heat-Shock Proteins - pharmacology ; MOLECULAR CLONING ; MUTANTS ; nonsense mutation ; NUCLEOTIDE SEQUENCE ; PCR ; Point Mutation ; Polymerase Chain Reaction ; PSI ; SACCHAROMYCES CEREVISIAE ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae - physiology ; Saccharomyces cerevisiae Proteins - antagonists & inhibitors ; Saccharomyces cerevisiae Proteins - pharmacology ; Saccharomyces cerevisiae Proteins - physiology ; suppressor ; THYMINE ; Transcription Factors - antagonists & inhibitors ; Transcription Factors - genetics ; Transcription Factors - physiology</subject><ispartof>Bioscience, biotechnology, and biochemistry, 2004-07, Vol.68 (7), p.1541-1548</ispartof><rights>2004 by Japan Society for Bioscience, Biotechnology, and Agrochemistry 2004</rights><rights>2004 INIST-CNRS</rights><rights>Copyright Japan Science and Technology Agency 2004</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c615t-ab159bd3d800518a9ab488e68a34418402707db5d0ccb2dbf5ac5c610d08de3d3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=16197143$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15277759$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Okazaki, H. (Teikyo Univ. of Science and Technology, Uenohara, Yamanashi (Japan))</creatorcontrib><creatorcontrib>Ono, B</creatorcontrib><creatorcontrib>Ohsumi, Y</creatorcontrib><creatorcontrib>Ohsumi, M</creatorcontrib><title>apg15-1, a UGA mutant allele in the Saccharomyces cerevisiae APG16 gene, and its suppression by a cytoplasmic factor</title><title>Bioscience, biotechnology, and biochemistry</title><addtitle>Biosci Biotechnol Biochem</addtitle><description>Autophagy is a complex cellular process by which starving cells utilize cytoplasmic macromolecules as nutritional resources. In Saccharomyces cerevisiaey more than 15 genes are involved in this process and most of them have been cloned and characterized by now. But there remains a complementation group represented by a single mutation, apg15-1 , unclear as to its molecular nature. We obtained DNA fragments that functionally complemented apg15-1 and found that the responsible ORF, YMR159C, was already assigned as APG16. It was further found that apg15-1 was a UGA allele in which the 243rd base of the 450 bp coding region o(APG16 was converted from C to T, and that the previously observed complementation between apg15-1 and apg16D was attributable to the action of a cytoplasmic omnipotent suppressor. This suppressor was readily cured by guanidine-HCl and also by overexpression or disruption of HSP104, indicating its close similarity to the PSI prion-like factor. Since apg15-1 is a mutation highly sensitive to termination suppression, it can be used as a tool to detect weak termination suppressors.</description><subject>Alleles</subject><subject>Aminopeptidases - antagonists & inhibitors</subject><subject>Aminopeptidases - physiology</subject><subject>autophagy</subject><subject>Autophagy - genetics</subject><subject>Autophagy - physiology</subject><subject>Autophagy-Related Proteins</subject><subject>Biological and medical sciences</subject><subject>Blotting, Western</subject><subject>Carrier Proteins - antagonists & inhibitors</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - physiology</subject><subject>Cloning, Molecular</subject><subject>Cvt pathway</subject><subject>CYTOPLASM</subject><subject>CYTOSINE</subject><subject>DNA, Bacterial - chemistry</subject><subject>DNA, Bacterial - genetics</subject><subject>EFFECTORS</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>GENES</subject><subject>Genetic Complementation Test</subject><subject>Guanidine - pharmacology</subject><subject>Heat-Shock Proteins - pharmacology</subject><subject>MOLECULAR CLONING</subject><subject>MUTANTS</subject><subject>nonsense mutation</subject><subject>NUCLEOTIDE SEQUENCE</subject><subject>PCR</subject><subject>Point Mutation</subject><subject>Polymerase Chain Reaction</subject><subject>PSI</subject><subject>SACCHAROMYCES CEREVISIAE</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae - physiology</subject><subject>Saccharomyces cerevisiae Proteins - antagonists & inhibitors</subject><subject>Saccharomyces cerevisiae Proteins - pharmacology</subject><subject>Saccharomyces cerevisiae Proteins - physiology</subject><subject>suppressor</subject><subject>THYMINE</subject><subject>Transcription Factors - antagonists & inhibitors</subject><subject>Transcription Factors - genetics</subject><subject>Transcription Factors - physiology</subject><issn>0916-8451</issn><issn>1347-6947</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0V2L1DAUBuAiijuuXnmtBERvtGNO89H0clh0VBZc0L0OJx-d7dI2NWmV_nuzzMiCCF4VwvOe9OQtiudAt1DV8N4Ys5VqC4LDg2IDjNelbHj9sNjQBmSpuICz4klKt5TmAwGPizMQVV3XotkUM04HECW8I0iu9zsyLDOOM8G-970n3UjmG0--obU3GMOwWp-I9dH_7FKHnuyu9iDJwY8-50dHujmRtExT9Cl1YSRmzWPtOoepxzR0lrRo5xCfFo9a7JN_dvqeF9cfP3y_-FReft1_vthdllaCmEs0IBrjmFOUClDYoOFKeamQcQ6K06qmtTPCUWtN5Uwr0IocpY4q55lj58Wb49wphh-LT7MeumR93-Pow5K0lDVreCX_C6v8dIxLmuGrv-BtWOKYl9DAeaNoLaHJ6u1R2RhSir7VU-wGjKsGqu8607kzLZW-6yzrl6eZixm8u7enkjJ4fQKYLPZtxNF26d7lK2vgLDt5dN3YhjjgrxB7p2dc-xD_hNi__-DFMdhi0HiI2X25yjuLvHUFjP0GrSe3_Q</recordid><startdate>20040701</startdate><enddate>20040701</enddate><creator>Okazaki, H. 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(Teikyo Univ. of Science and Technology, Uenohara, Yamanashi (Japan)) ; Ono, B ; Ohsumi, Y ; Ohsumi, M</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c615t-ab159bd3d800518a9ab488e68a34418402707db5d0ccb2dbf5ac5c610d08de3d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Alleles</topic><topic>Aminopeptidases - antagonists & inhibitors</topic><topic>Aminopeptidases - physiology</topic><topic>autophagy</topic><topic>Autophagy - genetics</topic><topic>Autophagy - physiology</topic><topic>Autophagy-Related Proteins</topic><topic>Biological and medical sciences</topic><topic>Blotting, Western</topic><topic>Carrier Proteins - antagonists & inhibitors</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - physiology</topic><topic>Cloning, Molecular</topic><topic>Cvt pathway</topic><topic>CYTOPLASM</topic><topic>CYTOSINE</topic><topic>DNA, Bacterial - chemistry</topic><topic>DNA, Bacterial - genetics</topic><topic>EFFECTORS</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>GENES</topic><topic>Genetic Complementation Test</topic><topic>Guanidine - pharmacology</topic><topic>Heat-Shock Proteins - pharmacology</topic><topic>MOLECULAR CLONING</topic><topic>MUTANTS</topic><topic>nonsense mutation</topic><topic>NUCLEOTIDE SEQUENCE</topic><topic>PCR</topic><topic>Point Mutation</topic><topic>Polymerase Chain Reaction</topic><topic>PSI</topic><topic>SACCHAROMYCES CEREVISIAE</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Saccharomyces cerevisiae - physiology</topic><topic>Saccharomyces cerevisiae Proteins - antagonists & inhibitors</topic><topic>Saccharomyces cerevisiae Proteins - pharmacology</topic><topic>Saccharomyces cerevisiae Proteins - physiology</topic><topic>suppressor</topic><topic>THYMINE</topic><topic>Transcription Factors - antagonists & inhibitors</topic><topic>Transcription Factors - genetics</topic><topic>Transcription Factors - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Okazaki, H. (Teikyo Univ. of Science and Technology, Uenohara, Yamanashi (Japan))</creatorcontrib><creatorcontrib>Ono, B</creatorcontrib><creatorcontrib>Ohsumi, Y</creatorcontrib><creatorcontrib>Ohsumi, M</creatorcontrib><collection>AGRIS</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>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Bioscience, biotechnology, and biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Okazaki, H. (Teikyo Univ. of Science and Technology, Uenohara, Yamanashi (Japan))</au><au>Ono, B</au><au>Ohsumi, Y</au><au>Ohsumi, M</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>apg15-1, a UGA mutant allele in the Saccharomyces cerevisiae APG16 gene, and its suppression by a cytoplasmic factor</atitle><jtitle>Bioscience, biotechnology, and biochemistry</jtitle><addtitle>Biosci Biotechnol Biochem</addtitle><date>2004-07-01</date><risdate>2004</risdate><volume>68</volume><issue>7</issue><spage>1541</spage><epage>1548</epage><pages>1541-1548</pages><issn>0916-8451</issn><eissn>1347-6947</eissn><abstract>Autophagy is a complex cellular process by which starving cells utilize cytoplasmic macromolecules as nutritional resources. In Saccharomyces cerevisiaey more than 15 genes are involved in this process and most of them have been cloned and characterized by now. But there remains a complementation group represented by a single mutation, apg15-1 , unclear as to its molecular nature. We obtained DNA fragments that functionally complemented apg15-1 and found that the responsible ORF, YMR159C, was already assigned as APG16. It was further found that apg15-1 was a UGA allele in which the 243rd base of the 450 bp coding region o(APG16 was converted from C to T, and that the previously observed complementation between apg15-1 and apg16D was attributable to the action of a cytoplasmic omnipotent suppressor. This suppressor was readily cured by guanidine-HCl and also by overexpression or disruption of HSP104, indicating its close similarity to the PSI prion-like factor. Since apg15-1 is a mutation highly sensitive to termination suppression, it can be used as a tool to detect weak termination suppressors.</abstract><cop>Tokyo</cop><pub>Japan Society for Bioscience, Biotechnology, and Agrochemistry</pub><pmid>15277759</pmid><doi>10.1271/bbb.68.1541</doi><tpages>8</tpages></addata></record> |
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| ispartof | Bioscience, biotechnology, and biochemistry, 2004-07, Vol.68 (7), p.1541-1548 |
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| source | J-STAGE Free; MEDLINE; Oxford University Press Journals All Titles (1996-Current); Open Access Titles of Japan; EZB-FREE-00999 freely available EZB journals; Free Full-Text Journals in Chemistry |
| subjects | Alleles Aminopeptidases - antagonists & inhibitors Aminopeptidases - physiology autophagy Autophagy - genetics Autophagy - physiology Autophagy-Related Proteins Biological and medical sciences Blotting, Western Carrier Proteins - antagonists & inhibitors Carrier Proteins - genetics Carrier Proteins - physiology Cloning, Molecular Cvt pathway CYTOPLASM CYTOSINE DNA, Bacterial - chemistry DNA, Bacterial - genetics EFFECTORS Fundamental and applied biological sciences. Psychology GENES Genetic Complementation Test Guanidine - pharmacology Heat-Shock Proteins - pharmacology MOLECULAR CLONING MUTANTS nonsense mutation NUCLEOTIDE SEQUENCE PCR Point Mutation Polymerase Chain Reaction PSI SACCHAROMYCES CEREVISIAE Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - physiology Saccharomyces cerevisiae Proteins - antagonists & inhibitors Saccharomyces cerevisiae Proteins - pharmacology Saccharomyces cerevisiae Proteins - physiology suppressor THYMINE Transcription Factors - antagonists & inhibitors Transcription Factors - genetics Transcription Factors - physiology |
| title | apg15-1, a UGA mutant allele in the Saccharomyces cerevisiae APG16 gene, and its suppression by a cytoplasmic factor |
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