A putative ATP-dependent RNA helicase involved in Saccharomyces cerevisiae ribosome assembly
We have isolated a cold-sensitive mutant of Saccharomyces cerevisiae in which there is a deficit of 60S ribosomal subunits. Cold sensitivity and the assembly defect are recessive and cosegregate, defining a single essential gene that we designate DRS1 (deficiency of ribosomal subunits). The wild-typ...
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Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1992-12, Vol.89 (23), p.11131-11135 |
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creator | Ripmaster, T.L. (Carnegie Mellon University, Pittsburgh, PA) Vaughan, G.P Woolford, J.L. Jr |
description | We have isolated a cold-sensitive mutant of Saccharomyces cerevisiae in which there is a deficit of 60S ribosomal subunits. Cold sensitivity and the assembly defect are recessive and cosegregate, defining a single essential gene that we designate DRS1 (deficiency of ribosomal subunits). The wild-type DRS1 gene was cloned by complementation of the cold-sensitive phenotype of drs1. Sequence analysis reveals a high degree of similarity to a family of proteins that are thought to function as ATP-dependent RNA helicases, Pulse-chase analysis of ribosomal RNA synthesis and processing indicates that the drs1 mutant accumulates the 27S precursor of the mature 25S rRNA. These results suggest that, as in pre-mRNA splicing, RNA helicase activities are involved in ribosomal RNA processing |
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(Carnegie Mellon University, Pittsburgh, PA) ; Vaughan, G.P ; Woolford, J.L. Jr</creator><creatorcontrib>Ripmaster, T.L. (Carnegie Mellon University, Pittsburgh, PA) ; Vaughan, G.P ; Woolford, J.L. Jr</creatorcontrib><description>We have isolated a cold-sensitive mutant of Saccharomyces cerevisiae in which there is a deficit of 60S ribosomal subunits. Cold sensitivity and the assembly defect are recessive and cosegregate, defining a single essential gene that we designate DRS1 (deficiency of ribosomal subunits). The wild-type DRS1 gene was cloned by complementation of the cold-sensitive phenotype of drs1. Sequence analysis reveals a high degree of similarity to a family of proteins that are thought to function as ATP-dependent RNA helicases, Pulse-chase analysis of ribosomal RNA synthesis and processing indicates that the drs1 mutant accumulates the 27S precursor of the mature 25S rRNA. These results suggest that, as in pre-mRNA splicing, RNA helicase activities are involved in ribosomal RNA processing</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.89.23.11131</identifier><identifier>PMID: 1454790</identifier><identifier>CODEN: PNASA6</identifier><language>eng</language><publisher>Washington, DC: National Academy of Sciences of the United States of America</publisher><subject>ACTIVIDAD ENZIMATICA ; ACTIVITE ENZYMATIQUE ; Amino Acid Sequence ; Amino acids ; ARN DE TRANSFERENCIA ; ARN DE TRANSFERT ; ARN RIBOSOMAL ; ARN RIBOSOMIAL ; Bacteria ; Base Sequence ; Biochemistry ; Biological and medical sciences ; Cell Nucleus - enzymology ; Cell structures and functions ; Cellular biology ; CLONACION ; CLONAGE ; DNA ; DNA, Fungal - genetics ; Fundamental and applied biological sciences. Psychology ; Genes, Fungal ; Genetic mutation ; Genomics ; LEVADURA ; LEVURE ; Molecular and cellular biology ; Molecular Sequence Data ; Morphogenesis ; MUTANT ; MUTANTES ; NUCLEOTIDE ; NUCLEOTIDOS ; Plasmids ; Restriction Mapping ; Ribonucleic acid ; Ribosomal proteins ; Ribosome ; Ribosomes ; Ribosomes - ultrastructure ; RNA ; RNA Helicases ; RNA Nucleotidyltransferases - metabolism ; RNA Processing, Post-Transcriptional ; RNA, Ribosomal - genetics ; SACCHAROMYCES CEREVISIAE ; Saccharomyces cerevisiae - enzymology ; Sequence Alignment ; Yeasts</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1992-12, Vol.89 (23), p.11131-11135</ispartof><rights>Copyright 1992 The National Academy of Sciences of the United States of America</rights><rights>1993 INIST-CNRS</rights><rights>Copyright National Academy of Sciences Dec 1, 1992</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c573t-7c72ac4312b64d08cfd862e85933072bfa87b2bcce06ed4ee8e7a335c3022d563</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/89/23.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/2360660$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/2360660$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27901,27902,53766,53768,57992,58225</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4528517$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1454790$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ripmaster, T.L. (Carnegie Mellon University, Pittsburgh, PA)</creatorcontrib><creatorcontrib>Vaughan, G.P</creatorcontrib><creatorcontrib>Woolford, J.L. Jr</creatorcontrib><title>A putative ATP-dependent RNA helicase involved in Saccharomyces cerevisiae ribosome assembly</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>We have isolated a cold-sensitive mutant of Saccharomyces cerevisiae in which there is a deficit of 60S ribosomal subunits. Cold sensitivity and the assembly defect are recessive and cosegregate, defining a single essential gene that we designate DRS1 (deficiency of ribosomal subunits). The wild-type DRS1 gene was cloned by complementation of the cold-sensitive phenotype of drs1. Sequence analysis reveals a high degree of similarity to a family of proteins that are thought to function as ATP-dependent RNA helicases, Pulse-chase analysis of ribosomal RNA synthesis and processing indicates that the drs1 mutant accumulates the 27S precursor of the mature 25S rRNA. These results suggest that, as in pre-mRNA splicing, RNA helicase activities are involved in ribosomal RNA processing</description><subject>ACTIVIDAD ENZIMATICA</subject><subject>ACTIVITE ENZYMATIQUE</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>ARN DE TRANSFERENCIA</subject><subject>ARN DE TRANSFERT</subject><subject>ARN RIBOSOMAL</subject><subject>ARN RIBOSOMIAL</subject><subject>Bacteria</subject><subject>Base Sequence</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Cell Nucleus - enzymology</subject><subject>Cell structures and functions</subject><subject>Cellular biology</subject><subject>CLONACION</subject><subject>CLONAGE</subject><subject>DNA</subject><subject>DNA, Fungal - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Genes, Fungal</subject><subject>Genetic mutation</subject><subject>Genomics</subject><subject>LEVADURA</subject><subject>LEVURE</subject><subject>Molecular and cellular biology</subject><subject>Molecular Sequence Data</subject><subject>Morphogenesis</subject><subject>MUTANT</subject><subject>MUTANTES</subject><subject>NUCLEOTIDE</subject><subject>NUCLEOTIDOS</subject><subject>Plasmids</subject><subject>Restriction Mapping</subject><subject>Ribonucleic acid</subject><subject>Ribosomal proteins</subject><subject>Ribosome</subject><subject>Ribosomes</subject><subject>Ribosomes - ultrastructure</subject><subject>RNA</subject><subject>RNA Helicases</subject><subject>RNA Nucleotidyltransferases - metabolism</subject><subject>RNA Processing, Post-Transcriptional</subject><subject>RNA, Ribosomal - genetics</subject><subject>SACCHAROMYCES CEREVISIAE</subject><subject>Saccharomyces cerevisiae - enzymology</subject><subject>Sequence Alignment</subject><subject>Yeasts</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkd2L1DAUxYso67j6LqJYRMSXjjdJ81HwZVj8gkXF3X0TQpre7mRomzFpB-e_N-OM4-qDPiVwfif33Jwse0hgTkCyV-vBxLmq5pTNCSGM3MpmBCpSiLKC29kMgMpClbS8m92LcQUAFVdwkp2Qkpeygln2dZGvp9GMboP54vJz0eAahwaHMf_ycZEvsXPWRMzdsPHdBpt0yS-MtUsTfL-1GHOLATcuOoN5cLWPvsfcxIh93W3vZ3da00V8cDhPs6u3by7P3hfnn959OFucF5ZLNhbSSmpsyQitRdmAsm2jBEXFK8ZA0ro1Sta0thZBYFMiKpSGMW4ZUNpwwU6z1_t311PdY2NT_GA6vQ6uN2GrvXH6T2VwS33tN5oDB5bsLw724L9NGEfdu2ix68yAfopaplm0ovBfkAhWcUp5Ap_9Ba78FIb0B5oCoVQxViUI9pANPsaA7TEwAb1rV-_a1arSlOmf7SbLk5uL_jbs60z684NuojVdG8xgXTxiJaeKE5mwlwdsN-CXemOQbqeuG_H7mNCn_0YT8XhPrOLowxGhTIAQu0iP9nJrvDbXIcW5ukjFEikE-wE_XdgI</recordid><startdate>19921201</startdate><enddate>19921201</enddate><creator>Ripmaster, T.L. (Carnegie Mellon University, Pittsburgh, PA)</creator><creator>Vaughan, G.P</creator><creator>Woolford, J.L. Jr</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>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>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>7X8</scope><scope>5PM</scope></search><sort><creationdate>19921201</creationdate><title>A putative ATP-dependent RNA helicase involved in Saccharomyces cerevisiae ribosome assembly</title><author>Ripmaster, T.L. (Carnegie Mellon University, Pittsburgh, PA) ; Vaughan, G.P ; Woolford, J.L. 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Psychology</topic><topic>Genes, Fungal</topic><topic>Genetic mutation</topic><topic>Genomics</topic><topic>LEVADURA</topic><topic>LEVURE</topic><topic>Molecular and cellular biology</topic><topic>Molecular Sequence Data</topic><topic>Morphogenesis</topic><topic>MUTANT</topic><topic>MUTANTES</topic><topic>NUCLEOTIDE</topic><topic>NUCLEOTIDOS</topic><topic>Plasmids</topic><topic>Restriction Mapping</topic><topic>Ribonucleic acid</topic><topic>Ribosomal proteins</topic><topic>Ribosome</topic><topic>Ribosomes</topic><topic>Ribosomes - ultrastructure</topic><topic>RNA</topic><topic>RNA Helicases</topic><topic>RNA Nucleotidyltransferases - metabolism</topic><topic>RNA Processing, Post-Transcriptional</topic><topic>RNA, Ribosomal - genetics</topic><topic>SACCHAROMYCES CEREVISIAE</topic><topic>Saccharomyces cerevisiae - enzymology</topic><topic>Sequence Alignment</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ripmaster, T.L. 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(Carnegie Mellon University, Pittsburgh, PA)</au><au>Vaughan, G.P</au><au>Woolford, J.L. Jr</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A putative ATP-dependent RNA helicase involved in Saccharomyces cerevisiae ribosome assembly</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1992-12-01</date><risdate>1992</risdate><volume>89</volume><issue>23</issue><spage>11131</spage><epage>11135</epage><pages>11131-11135</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><coden>PNASA6</coden><abstract>We have isolated a cold-sensitive mutant of Saccharomyces cerevisiae in which there is a deficit of 60S ribosomal subunits. Cold sensitivity and the assembly defect are recessive and cosegregate, defining a single essential gene that we designate DRS1 (deficiency of ribosomal subunits). The wild-type DRS1 gene was cloned by complementation of the cold-sensitive phenotype of drs1. Sequence analysis reveals a high degree of similarity to a family of proteins that are thought to function as ATP-dependent RNA helicases, Pulse-chase analysis of ribosomal RNA synthesis and processing indicates that the drs1 mutant accumulates the 27S precursor of the mature 25S rRNA. These results suggest that, as in pre-mRNA splicing, RNA helicase activities are involved in ribosomal RNA processing</abstract><cop>Washington, DC</cop><pub>National Academy of Sciences of the United States of America</pub><pmid>1454790</pmid><doi>10.1073/pnas.89.23.11131</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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subjects | ACTIVIDAD ENZIMATICA ACTIVITE ENZYMATIQUE Amino Acid Sequence Amino acids ARN DE TRANSFERENCIA ARN DE TRANSFERT ARN RIBOSOMAL ARN RIBOSOMIAL Bacteria Base Sequence Biochemistry Biological and medical sciences Cell Nucleus - enzymology Cell structures and functions Cellular biology CLONACION CLONAGE DNA DNA, Fungal - genetics Fundamental and applied biological sciences. Psychology Genes, Fungal Genetic mutation Genomics LEVADURA LEVURE Molecular and cellular biology Molecular Sequence Data Morphogenesis MUTANT MUTANTES NUCLEOTIDE NUCLEOTIDOS Plasmids Restriction Mapping Ribonucleic acid Ribosomal proteins Ribosome Ribosomes Ribosomes - ultrastructure RNA RNA Helicases RNA Nucleotidyltransferases - metabolism RNA Processing, Post-Transcriptional RNA, Ribosomal - genetics SACCHAROMYCES CEREVISIAE Saccharomyces cerevisiae - enzymology Sequence Alignment Yeasts |
title | A putative ATP-dependent RNA helicase involved in Saccharomyces cerevisiae ribosome assembly |
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