multisubunit 3' end processing factor from yeast containing poly(A) polymerase and homologues of the subunits of mammalian cleavage and polyadenylation specificity factor
Polyadenylation is the second step in 3′ end formation of most eukaryotic mRNAs. In Saccharomyces cerevisiae , this step requires three trans ‐acting factors: poly(A) polymerase (Pap1p), cleavage factor I (CF I) and polyadenylation factor I (PF I). Here, we describe the purification and subunit comp...
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| Veröffentlicht in: | The EMBO journal 1997-08, Vol.16 (15), p.4727-4737 |
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| creator | Preker, P.J Ohnacker, M Minivielle-Sebastia, L Keller, W |
| description | Polyadenylation is the second step in 3′ end formation of most eukaryotic mRNAs. In
Saccharomyces cerevisiae
, this step requires three
trans
‐acting factors: poly(A) polymerase (Pap1p), cleavage factor I (CF I) and polyadenylation factor I (PF I). Here, we describe the purification and subunit composition of a multiprotein complex containing Pap1p and PF I activities. PF I–Pap1p was purified to homogeneity by complementation of extracts mutant in the Fip1p subunit of PF I. In addition to Fip1p and Pap1p, the factor comprises homologues of all four subunits of mammalian cleavage and polyadenylation specificity factor (CPSF), as well as Pta1p, which previously has been implicated in pre‐tRNA processing, and several as yet uncharacterized proteins. As expected for a PF I subunit,
pta1‐1
mutant extracts are deficient for polyadenylation
in vitro
. PF I also appears to be functionally related to CPSF, as it polyadenylates a substrate RNA more efficiently than Pap1p alone. Possibly, the observed interaction of the complex with RNA tethers Pap1p to its substrate. |
| doi_str_mv | 10.1093/emboj/16.15.4727 |
| format | Article |
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Saccharomyces cerevisiae
, this step requires three
trans
‐acting factors: poly(A) polymerase (Pap1p), cleavage factor I (CF I) and polyadenylation factor I (PF I). Here, we describe the purification and subunit composition of a multiprotein complex containing Pap1p and PF I activities. PF I–Pap1p was purified to homogeneity by complementation of extracts mutant in the Fip1p subunit of PF I. In addition to Fip1p and Pap1p, the factor comprises homologues of all four subunits of mammalian cleavage and polyadenylation specificity factor (CPSF), as well as Pta1p, which previously has been implicated in pre‐tRNA processing, and several as yet uncharacterized proteins. As expected for a PF I subunit,
pta1‐1
mutant extracts are deficient for polyadenylation
in vitro
. PF I also appears to be functionally related to CPSF, as it polyadenylates a substrate RNA more efficiently than Pap1p alone. Possibly, the observed interaction of the complex with RNA tethers Pap1p to its substrate.</description><identifier>ISSN: 0261-4189</identifier><identifier>ISSN: 1460-2075</identifier><identifier>EISSN: 1460-2075</identifier><identifier>DOI: 10.1093/emboj/16.15.4727</identifier><identifier>PMID: 9303317</identifier><language>eng</language><publisher>Chichester, UK: John Wiley & Sons, Ltd</publisher><subject>Amino Acid Sequence ; Animals ; Base Sequence ; binding proteins ; Biochemistry, Molecular Biology ; chemical reactions ; DNA Primers - genetics ; Evolution, Molecular ; Fungal Proteins - chemistry ; Fungal Proteins - genetics ; Fungal Proteins - metabolism ; Genes, Fungal ; Life Sciences ; Macromolecular Substances ; messenger RNA ; Molecular Sequence Data ; mRNA Cleavage and Polyadenylation Factors ; Multiprotein Complexes ; Mutation ; nucleotidyltransferases ; poly(A) polymerase holoenzyme ; polyadenylation factor I ; Polynucleotide Adenylyltransferase - chemistry ; Polynucleotide Adenylyltransferase - genetics ; Polynucleotide Adenylyltransferase - metabolism ; polypeptides ; pre-messenger RNA 3′ end processing ; precursors ; Protein Conformation ; purification ; RNA Processing, Post-Transcriptional ; RNA, Fungal - biosynthesis ; RNA, Messenger - biosynthesis ; RNA-Binding Proteins - chemistry ; RNA-Binding Proteins - genetics ; RNA-Binding Proteins - metabolism ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins ; Substrate Specificity ; yeast</subject><ispartof>The EMBO journal, 1997-08, Vol.16 (15), p.4727-4737</ispartof><rights>European Molecular Biology Organization 1997</rights><rights>Copyright © 1997 European Molecular Biology Organization</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c6321-1066daceb7b8c58a7df806bfe5cc3d4e62f2cee5d3c59ce517d74a2456462a713</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1170099/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1170099/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,1417,1433,27924,27925,45574,45575,46409,46833,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9303317$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-02473933$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Preker, P.J</creatorcontrib><creatorcontrib>Ohnacker, M</creatorcontrib><creatorcontrib>Minivielle-Sebastia, L</creatorcontrib><creatorcontrib>Keller, W</creatorcontrib><title>multisubunit 3' end processing factor from yeast containing poly(A) polymerase and homologues of the subunits of mammalian cleavage and polyadenylation specificity factor</title><title>The EMBO journal</title><addtitle>EMBO J</addtitle><addtitle>EMBO J</addtitle><description>Polyadenylation is the second step in 3′ end formation of most eukaryotic mRNAs. In
Saccharomyces cerevisiae
, this step requires three
trans
‐acting factors: poly(A) polymerase (Pap1p), cleavage factor I (CF I) and polyadenylation factor I (PF I). Here, we describe the purification and subunit composition of a multiprotein complex containing Pap1p and PF I activities. PF I–Pap1p was purified to homogeneity by complementation of extracts mutant in the Fip1p subunit of PF I. In addition to Fip1p and Pap1p, the factor comprises homologues of all four subunits of mammalian cleavage and polyadenylation specificity factor (CPSF), as well as Pta1p, which previously has been implicated in pre‐tRNA processing, and several as yet uncharacterized proteins. As expected for a PF I subunit,
pta1‐1
mutant extracts are deficient for polyadenylation
in vitro
. PF I also appears to be functionally related to CPSF, as it polyadenylates a substrate RNA more efficiently than Pap1p alone. Possibly, the observed interaction of the complex with RNA tethers Pap1p to its substrate.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>binding proteins</subject><subject>Biochemistry, Molecular Biology</subject><subject>chemical reactions</subject><subject>DNA Primers - genetics</subject><subject>Evolution, Molecular</subject><subject>Fungal Proteins - chemistry</subject><subject>Fungal Proteins - genetics</subject><subject>Fungal Proteins - metabolism</subject><subject>Genes, Fungal</subject><subject>Life Sciences</subject><subject>Macromolecular Substances</subject><subject>messenger RNA</subject><subject>Molecular Sequence Data</subject><subject>mRNA Cleavage and Polyadenylation Factors</subject><subject>Multiprotein Complexes</subject><subject>Mutation</subject><subject>nucleotidyltransferases</subject><subject>poly(A) polymerase holoenzyme</subject><subject>polyadenylation factor I</subject><subject>Polynucleotide Adenylyltransferase - chemistry</subject><subject>Polynucleotide Adenylyltransferase - genetics</subject><subject>Polynucleotide Adenylyltransferase - metabolism</subject><subject>polypeptides</subject><subject>pre-messenger RNA 3′ end processing</subject><subject>precursors</subject><subject>Protein Conformation</subject><subject>purification</subject><subject>RNA Processing, Post-Transcriptional</subject><subject>RNA, Fungal - biosynthesis</subject><subject>RNA, Messenger - biosynthesis</subject><subject>RNA-Binding Proteins - chemistry</subject><subject>RNA-Binding Proteins - genetics</subject><subject>RNA-Binding Proteins - metabolism</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>Substrate Specificity</subject><subject>yeast</subject><issn>0261-4189</issn><issn>1460-2075</issn><issn>1460-2075</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNUk1v0zAYjhBolMGdC8InYId2_ojt5ILUTaODFTiwCYmL5TpvWo_ELnZS6F_iV5I0Vfm4jJNlPx_vh58keUrwhOCcnUK98LenREwIn6SSynvJiKQCjymW_H4ywlSQcUqy_GHyKMZbjDHPJDlKjnKGGSNylPys26qxsV20zjaIvUTgCrQO3kCM1i1RqU3jAyqDr9EWdGyQ8a7R1vXg2lfbV9OT3VlD0BGQ7uQrX_vKL1uIyJeoWQHa--_uta5rXVntkKlAb_RyEPUeugC3rXRjvUNxDcaW1thmu2_icfKg1FWEJ_vzOLl5c3F9fjmef5y9PZ_Ox0YwSsYEC1FoAwu5yAzPtCzKDItFCdwYVqQgaEkNAC-Y4bkBTmQhU01TLlJBtSTsOHk9-K7bRQ2FAdcEXal1sLUOW-W1VX8jzq7U0m8UIRLjPO8MTgaD1T-yy-lc9W-YppLljG36Yi_2xYL_1m2sUbWNBqpKO_BtVDKnWUZFeieRCJyTLMMdEQ9EE3yMAcpDCwSrPjRqF5pOoAhXfWg6ybM_Jz4I9inp8HzAv9sKtnf6qYv3Z-8kz3HK-wHJoI2dzC0hqFvfBtd94H_043TTBjgU_O05HnAbG_hxgHX4qoRkkqvPH2bqen715exqhlW_u-cDv9Re6WWwUd18opgwTDOZcpyxX7KdB8g</recordid><startdate>19970801</startdate><enddate>19970801</enddate><creator>Preker, P.J</creator><creator>Ohnacker, M</creator><creator>Minivielle-Sebastia, L</creator><creator>Keller, W</creator><general>John Wiley & Sons, Ltd</general><general>Nature Publishing Group UK</general><general>EMBO Press</general><scope>FBQ</scope><scope>BSCLL</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>7TM</scope><scope>M7N</scope><scope>7X8</scope><scope>1XC</scope><scope>5PM</scope></search><sort><creationdate>19970801</creationdate><title>multisubunit 3' end processing factor from yeast containing poly(A) polymerase and homologues of the subunits of mammalian cleavage and polyadenylation specificity factor</title><author>Preker, P.J ; Ohnacker, M ; Minivielle-Sebastia, L ; Keller, W</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c6321-1066daceb7b8c58a7df806bfe5cc3d4e62f2cee5d3c59ce517d74a2456462a713</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>binding proteins</topic><topic>Biochemistry, Molecular Biology</topic><topic>chemical reactions</topic><topic>DNA Primers - genetics</topic><topic>Evolution, Molecular</topic><topic>Fungal Proteins - chemistry</topic><topic>Fungal Proteins - genetics</topic><topic>Fungal Proteins - metabolism</topic><topic>Genes, Fungal</topic><topic>Life Sciences</topic><topic>Macromolecular Substances</topic><topic>messenger RNA</topic><topic>Molecular Sequence Data</topic><topic>mRNA Cleavage and Polyadenylation Factors</topic><topic>Multiprotein Complexes</topic><topic>Mutation</topic><topic>nucleotidyltransferases</topic><topic>poly(A) polymerase holoenzyme</topic><topic>polyadenylation factor I</topic><topic>Polynucleotide Adenylyltransferase - chemistry</topic><topic>Polynucleotide Adenylyltransferase - genetics</topic><topic>Polynucleotide Adenylyltransferase - metabolism</topic><topic>polypeptides</topic><topic>pre-messenger RNA 3′ end processing</topic><topic>precursors</topic><topic>Protein Conformation</topic><topic>purification</topic><topic>RNA Processing, Post-Transcriptional</topic><topic>RNA, Fungal - biosynthesis</topic><topic>RNA, Messenger - biosynthesis</topic><topic>RNA-Binding Proteins - chemistry</topic><topic>RNA-Binding Proteins - genetics</topic><topic>RNA-Binding Proteins - metabolism</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Saccharomyces cerevisiae Proteins</topic><topic>Substrate Specificity</topic><topic>yeast</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Preker, P.J</creatorcontrib><creatorcontrib>Ohnacker, M</creatorcontrib><creatorcontrib>Minivielle-Sebastia, L</creatorcontrib><creatorcontrib>Keller, W</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>MEDLINE - Academic</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The EMBO journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Preker, P.J</au><au>Ohnacker, M</au><au>Minivielle-Sebastia, L</au><au>Keller, W</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>multisubunit 3' end processing factor from yeast containing poly(A) polymerase and homologues of the subunits of mammalian cleavage and polyadenylation specificity factor</atitle><jtitle>The EMBO journal</jtitle><stitle>EMBO J</stitle><addtitle>EMBO J</addtitle><date>1997-08-01</date><risdate>1997</risdate><volume>16</volume><issue>15</issue><spage>4727</spage><epage>4737</epage><pages>4727-4737</pages><issn>0261-4189</issn><issn>1460-2075</issn><eissn>1460-2075</eissn><abstract>Polyadenylation is the second step in 3′ end formation of most eukaryotic mRNAs. In
Saccharomyces cerevisiae
, this step requires three
trans
‐acting factors: poly(A) polymerase (Pap1p), cleavage factor I (CF I) and polyadenylation factor I (PF I). Here, we describe the purification and subunit composition of a multiprotein complex containing Pap1p and PF I activities. PF I–Pap1p was purified to homogeneity by complementation of extracts mutant in the Fip1p subunit of PF I. In addition to Fip1p and Pap1p, the factor comprises homologues of all four subunits of mammalian cleavage and polyadenylation specificity factor (CPSF), as well as Pta1p, which previously has been implicated in pre‐tRNA processing, and several as yet uncharacterized proteins. As expected for a PF I subunit,
pta1‐1
mutant extracts are deficient for polyadenylation
in vitro
. PF I also appears to be functionally related to CPSF, as it polyadenylates a substrate RNA more efficiently than Pap1p alone. Possibly, the observed interaction of the complex with RNA tethers Pap1p to its substrate.</abstract><cop>Chichester, UK</cop><pub>John Wiley & Sons, Ltd</pub><pmid>9303317</pmid><doi>10.1093/emboj/16.15.4727</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| issn | 0261-4189 1460-2075 1460-2075 |
| language | eng |
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| source | MEDLINE; Wiley Journals; Wiley Online Library Free Content; EZB-FREE-00999 freely available EZB journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Sequence Animals Base Sequence binding proteins Biochemistry, Molecular Biology chemical reactions DNA Primers - genetics Evolution, Molecular Fungal Proteins - chemistry Fungal Proteins - genetics Fungal Proteins - metabolism Genes, Fungal Life Sciences Macromolecular Substances messenger RNA Molecular Sequence Data mRNA Cleavage and Polyadenylation Factors Multiprotein Complexes Mutation nucleotidyltransferases poly(A) polymerase holoenzyme polyadenylation factor I Polynucleotide Adenylyltransferase - chemistry Polynucleotide Adenylyltransferase - genetics Polynucleotide Adenylyltransferase - metabolism polypeptides pre-messenger RNA 3′ end processing precursors Protein Conformation purification RNA Processing, Post-Transcriptional RNA, Fungal - biosynthesis RNA, Messenger - biosynthesis RNA-Binding Proteins - chemistry RNA-Binding Proteins - genetics RNA-Binding Proteins - metabolism Saccharomyces cerevisiae Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins Substrate Specificity yeast |
| title | multisubunit 3' end processing factor from yeast containing poly(A) polymerase and homologues of the subunits of mammalian cleavage and polyadenylation specificity factor |
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