Association of the Est1 protein with telomerase activity in yeast
The est1 mutant was previously identified because it is defective in telomere maintenance and displays a senescent phenotype. To see if Est1 might be a component of yeast telomerase, we examined immunoprecipitated Est1. The yeast telomerase RNA Tlc1 specifically coprecipitated with Est1. Furthermore...
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Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1996-04, Vol.93 (7), p.2817-2821 |
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description | The est1 mutant was previously identified because it is defective in telomere maintenance and displays a senescent phenotype. To see if Est1 might be a component of yeast telomerase, we examined immunoprecipitated Est1. The yeast telomerase RNA Tlc1 specifically coprecipitated with Est1. Furthermore, the Est1 immunoprecipitates contained a telomerase-like activity. As expected for yeast telomerase, the activity elongated telomeric primers, it required dGTP and dTTP but not dATP or dCTP, and it was sensitive to RNase A. Further evidence suggesting that the activity was telomerase was obtained from experiments using a TLC1-1 mutant strain, which has a mutant telomerase template containing dG residues. The activity immunoprecipitated from TLC1-1 mutant strains incorporated 32P-labeled dCTP, while activity from TLC1 strains did not. Use of different telomeric primer substrates revealed two distinguishable telomerase-like activities: one was dependent on TLC1, and one was not. The TLC1-independent activity may be due to a second yeast telomerase RNA, or it may be some other kind of activity. |
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To see if Est1 might be a component of yeast telomerase, we examined immunoprecipitated Est1. The yeast telomerase RNA Tlc1 specifically coprecipitated with Est1. Furthermore, the Est1 immunoprecipitates contained a telomerase-like activity. As expected for yeast telomerase, the activity elongated telomeric primers, it required dGTP and dTTP but not dATP or dCTP, and it was sensitive to RNase A. Further evidence suggesting that the activity was telomerase was obtained from experiments using a TLC1-1 mutant strain, which has a mutant telomerase template containing dG residues. The activity immunoprecipitated from TLC1-1 mutant strains incorporated 32P-labeled dCTP, while activity from TLC1 strains did not. Use of different telomeric primer substrates revealed two distinguishable telomerase-like activities: one was dependent on TLC1, and one was not. The TLC1-independent activity may be due to a second yeast telomerase RNA, or it may be some other kind of activity.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.93.7.2817</identifier><identifier>PMID: 8610124</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>actividad enzimatica ; activite enzymatique ; adn ; Amino Acid Sequence ; Base Sequence ; Biochemistry ; Blotting, Northern ; Cellular senescence ; Centrifugation ; chromosome ; chromosomes ; cromosomas ; Deoxyguanosine ; dna ; Enzymes ; enzymic activity ; Fungal Proteins - isolation & purification ; Fungal Proteins - metabolism ; Kinetics ; Molecular Sequence Data ; Mutagenesis ; mutant ; mutantes ; mutants ; Mutation ; nucleotide ; Nucleotides ; nucleotidos ; Oligodeoxyribonucleotides - chemistry ; Oligodeoxyribonucleotides - metabolism ; Oligonucleotides ; Phenotypes ; pirimidinas ; Plasmids ; Proteins ; purificacion ; purification ; pyrimidine ; pyrimidines ; RNA ; RNA, Fungal - biosynthesis ; RNA, Fungal - isolation & purification ; RNA, Fungal - metabolism ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - enzymology ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae Proteins ; Substrate Specificity ; Telomerase - isolation & purification ; Telomerase - metabolism ; Telomeres ; Templates, Genetic ; thymidine ; timidina ; transferasas ; transferase ; transferases ; Yeast ; Yeasts</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1996-04, Vol.93 (7), p.2817-2821</ispartof><rights>Copyright 1996 National Academy of Sciences</rights><rights>Copyright National Academy of Sciences Apr 2, 1996</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c536t-b97ec8ae6d963f7cec9d7527fd623b38b5c9b7cf713c758c84760a7d63c9c33</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/93/7.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/39070$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/39070$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27924,27925,53791,53793,58017,58250</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8610124$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Steiner, Barbara R.</creatorcontrib><creatorcontrib>Hidaka, Kyoko</creatorcontrib><creatorcontrib>Futcher, Bruce</creatorcontrib><creatorcontrib>Cold Spring Harbor Laboratory, Cold Spring Harbor, NY</creatorcontrib><title>Association of the Est1 protein with telomerase activity in yeast</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The est1 mutant was previously identified because it is defective in telomere maintenance and displays a senescent phenotype. To see if Est1 might be a component of yeast telomerase, we examined immunoprecipitated Est1. The yeast telomerase RNA Tlc1 specifically coprecipitated with Est1. Furthermore, the Est1 immunoprecipitates contained a telomerase-like activity. As expected for yeast telomerase, the activity elongated telomeric primers, it required dGTP and dTTP but not dATP or dCTP, and it was sensitive to RNase A. Further evidence suggesting that the activity was telomerase was obtained from experiments using a TLC1-1 mutant strain, which has a mutant telomerase template containing dG residues. The activity immunoprecipitated from TLC1-1 mutant strains incorporated 32P-labeled dCTP, while activity from TLC1 strains did not. Use of different telomeric primer substrates revealed two distinguishable telomerase-like activities: one was dependent on TLC1, and one was not. The TLC1-independent activity may be due to a second yeast telomerase RNA, or it may be some other kind of activity.</description><subject>actividad enzimatica</subject><subject>activite enzymatique</subject><subject>adn</subject><subject>Amino Acid Sequence</subject><subject>Base Sequence</subject><subject>Biochemistry</subject><subject>Blotting, Northern</subject><subject>Cellular senescence</subject><subject>Centrifugation</subject><subject>chromosome</subject><subject>chromosomes</subject><subject>cromosomas</subject><subject>Deoxyguanosine</subject><subject>dna</subject><subject>Enzymes</subject><subject>enzymic activity</subject><subject>Fungal Proteins - isolation & purification</subject><subject>Fungal Proteins - metabolism</subject><subject>Kinetics</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis</subject><subject>mutant</subject><subject>mutantes</subject><subject>mutants</subject><subject>Mutation</subject><subject>nucleotide</subject><subject>Nucleotides</subject><subject>nucleotidos</subject><subject>Oligodeoxyribonucleotides - chemistry</subject><subject>Oligodeoxyribonucleotides - metabolism</subject><subject>Oligonucleotides</subject><subject>Phenotypes</subject><subject>pirimidinas</subject><subject>Plasmids</subject><subject>Proteins</subject><subject>purificacion</subject><subject>purification</subject><subject>pyrimidine</subject><subject>pyrimidines</subject><subject>RNA</subject><subject>RNA, Fungal - biosynthesis</subject><subject>RNA, Fungal - isolation & purification</subject><subject>RNA, Fungal - metabolism</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - enzymology</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>Substrate Specificity</subject><subject>Telomerase - isolation & purification</subject><subject>Telomerase - metabolism</subject><subject>Telomeres</subject><subject>Templates, Genetic</subject><subject>thymidine</subject><subject>timidina</subject><subject>transferasas</subject><subject>transferase</subject><subject>transferases</subject><subject>Yeast</subject><subject>Yeasts</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kU2P0zAQhi0EWsrClQMSKOKwtwQ7Tjy2tJdqtXxIK3FYOFuOM9m6SuNiOwv997hqqQoHTnN4ntea8UvIa0YrRoF_2E4mVopXUNWSwROyYFSxUjSKPiULSmsoZVM3z8mLGNeUUtVKekEupGCU1c2CLJcxeutMcn4q_FCkFRa3MbFiG3xCNxU_XVoVCUe_wWAiFsYm9-jSrshshyaml-TZYMaIr47zktx_vP1287m8-_rpy83yrrQtF6nsFKCVBkWvBB_AolU9tDUMvah5x2XXWtWBHYBxC620sgFBDfSCW2U5vyTXh1e3c7fB3uKUghn1NriNCTvtjdN_k8mt9IN_1FwBEzl-dYwH_2PGmPTGRYvjaCb0c9QMaNOChCy-_0dc-zlM-TBd5x-TLeN1lqqDZIOPMeBw2oNRvW9F71vRimvQ-1Zy4O359if9WMMZ3-f-0PP81f-4HuZxTPgrZfHNQVzH5MPJ5IoCzfDdAQ7Ga_MQXNTf75lSgjLe5Bb4b7uhswc</recordid><startdate>19960402</startdate><enddate>19960402</enddate><creator>Steiner, Barbara R.</creator><creator>Hidaka, Kyoko</creator><creator>Futcher, Bruce</creator><general>National Academy of Sciences of the United States of America</general><general>National Acad Sciences</general><general>National Academy of Sciences</general><scope>FBQ</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>5PM</scope></search><sort><creationdate>19960402</creationdate><title>Association of the Est1 protein with telomerase activity in yeast</title><author>Steiner, Barbara R. ; Hidaka, Kyoko ; Futcher, Bruce</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c536t-b97ec8ae6d963f7cec9d7527fd623b38b5c9b7cf713c758c84760a7d63c9c33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>actividad enzimatica</topic><topic>activite enzymatique</topic><topic>adn</topic><topic>Amino Acid Sequence</topic><topic>Base Sequence</topic><topic>Biochemistry</topic><topic>Blotting, Northern</topic><topic>Cellular senescence</topic><topic>Centrifugation</topic><topic>chromosome</topic><topic>chromosomes</topic><topic>cromosomas</topic><topic>Deoxyguanosine</topic><topic>dna</topic><topic>Enzymes</topic><topic>enzymic activity</topic><topic>Fungal Proteins - isolation & purification</topic><topic>Fungal Proteins - metabolism</topic><topic>Kinetics</topic><topic>Molecular Sequence Data</topic><topic>Mutagenesis</topic><topic>mutant</topic><topic>mutantes</topic><topic>mutants</topic><topic>Mutation</topic><topic>nucleotide</topic><topic>Nucleotides</topic><topic>nucleotidos</topic><topic>Oligodeoxyribonucleotides - chemistry</topic><topic>Oligodeoxyribonucleotides - metabolism</topic><topic>Oligonucleotides</topic><topic>Phenotypes</topic><topic>pirimidinas</topic><topic>Plasmids</topic><topic>Proteins</topic><topic>purificacion</topic><topic>purification</topic><topic>pyrimidine</topic><topic>pyrimidines</topic><topic>RNA</topic><topic>RNA, Fungal - biosynthesis</topic><topic>RNA, Fungal - isolation & purification</topic><topic>RNA, Fungal - metabolism</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - enzymology</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Saccharomyces cerevisiae Proteins</topic><topic>Substrate Specificity</topic><topic>Telomerase - isolation & purification</topic><topic>Telomerase - metabolism</topic><topic>Telomeres</topic><topic>Templates, Genetic</topic><topic>thymidine</topic><topic>timidina</topic><topic>transferasas</topic><topic>transferase</topic><topic>transferases</topic><topic>Yeast</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Steiner, Barbara R.</creatorcontrib><creatorcontrib>Hidaka, Kyoko</creatorcontrib><creatorcontrib>Futcher, Bruce</creatorcontrib><creatorcontrib>Cold Spring Harbor Laboratory, Cold Spring Harbor, NY</creatorcontrib><collection>AGRIS</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Steiner, Barbara R.</au><au>Hidaka, Kyoko</au><au>Futcher, Bruce</au><aucorp>Cold Spring Harbor Laboratory, Cold Spring Harbor, NY</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Association of the Est1 protein with telomerase activity in yeast</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1996-04-02</date><risdate>1996</risdate><volume>93</volume><issue>7</issue><spage>2817</spage><epage>2821</epage><pages>2817-2821</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>The est1 mutant was previously identified because it is defective in telomere maintenance and displays a senescent phenotype. To see if Est1 might be a component of yeast telomerase, we examined immunoprecipitated Est1. The yeast telomerase RNA Tlc1 specifically coprecipitated with Est1. Furthermore, the Est1 immunoprecipitates contained a telomerase-like activity. As expected for yeast telomerase, the activity elongated telomeric primers, it required dGTP and dTTP but not dATP or dCTP, and it was sensitive to RNase A. Further evidence suggesting that the activity was telomerase was obtained from experiments using a TLC1-1 mutant strain, which has a mutant telomerase template containing dG residues. The activity immunoprecipitated from TLC1-1 mutant strains incorporated 32P-labeled dCTP, while activity from TLC1 strains did not. Use of different telomeric primer substrates revealed two distinguishable telomerase-like activities: one was dependent on TLC1, and one was not. The TLC1-independent activity may be due to a second yeast telomerase RNA, or it may be some other kind of activity.</abstract><cop>United States</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>8610124</pmid><doi>10.1073/pnas.93.7.2817</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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subjects | actividad enzimatica activite enzymatique adn Amino Acid Sequence Base Sequence Biochemistry Blotting, Northern Cellular senescence Centrifugation chromosome chromosomes cromosomas Deoxyguanosine dna Enzymes enzymic activity Fungal Proteins - isolation & purification Fungal Proteins - metabolism Kinetics Molecular Sequence Data Mutagenesis mutant mutantes mutants Mutation nucleotide Nucleotides nucleotidos Oligodeoxyribonucleotides - chemistry Oligodeoxyribonucleotides - metabolism Oligonucleotides Phenotypes pirimidinas Plasmids Proteins purificacion purification pyrimidine pyrimidines RNA RNA, Fungal - biosynthesis RNA, Fungal - isolation & purification RNA, Fungal - metabolism Saccharomyces cerevisiae Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae Proteins Substrate Specificity Telomerase - isolation & purification Telomerase - metabolism Telomeres Templates, Genetic thymidine timidina transferasas transferase transferases Yeast Yeasts |
title | Association of the Est1 protein with telomerase activity in yeast |
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