Phosphorylated Ser/Arg-Rich Proteins: Limiting Factors in the Assembly of 200S Large Nuclear Ribonucleoprotein Particles
We have previously shown that specific nuclear pre-mRNA transcripts and their splicing products, as well as the general population of nuclear poly(A)+ RNA, are packaged in large nuclear ribonucleoprotein (lnRNP) particles that sediment at the 200S region in sucrose gradients. The lnRNP particles con...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 1996-08, Vol.93 (17), p.8830-8835 |
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| creator | Yitzhaki, Shmuel Miriami, Elana Sperling, Ruth Sperling, Joseph |
| description | We have previously shown that specific nuclear pre-mRNA transcripts and their splicing products, as well as the general population of nuclear poly(A)+ RNA, are packaged in large nuclear ribonucleoprotein (lnRNP) particles that sediment at the 200S region in sucrose gradients. The lnRNP particles contain all uridine-rich small nuclear ribonucleoprotein complexes required for pre-mRNA splicing, as well as protein splicing factors. In this paper we show that all of the phosphorylated, mAb 104 detectable, Ser/Arg-rich essential splicing factors (SR proteins) in the nucleoplasm are integral components of the lnRNP particles, whereas only part of the essential splicing factor U2AF65 (U2 snRNP auxiliary factor) and the polypyrimidine tract binding protein (PTB) are associated with these particles. This finding suggests a limiting role for SR proteins in the assembly of the lnRNP particles. We further show that the structural integrity of lnRNP particles is sensitive to variations in the phosphorylation levels of the SR proteins. |
| doi_str_mv | 10.1073/pnas.93.17.8830 |
| format | Article |
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The lnRNP particles contain all uridine-rich small nuclear ribonucleoprotein complexes required for pre-mRNA splicing, as well as protein splicing factors. In this paper we show that all of the phosphorylated, mAb 104 detectable, Ser/Arg-rich essential splicing factors (SR proteins) in the nucleoplasm are integral components of the lnRNP particles, whereas only part of the essential splicing factor U2AF65 (U2 snRNP auxiliary factor) and the polypyrimidine tract binding protein (PTB) are associated with these particles. This finding suggests a limiting role for SR proteins in the assembly of the lnRNP particles. We further show that the structural integrity of lnRNP particles is sensitive to variations in the phosphorylation levels of the SR proteins.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.93.17.8830</identifier><identifier>PMID: 8799112</identifier><language>eng</language><publisher>United States: National Academy of Sciences of the United States of America</publisher><subject>Animals ; Aspartate Carbamoyltransferase - genetics ; Cell Nucleus - metabolism ; Cricetinae ; Dihydroorotase - genetics ; DNA-Binding Proteins - analysis ; Gels ; HeLa Cells ; Humans ; Ligases - genetics ; Nuclear Proteins - chemistry ; Phosphoproteins - analysis ; Phosphorylation ; Polypyrimidine Tract-Binding Protein ; Precipitin Tests ; Protein Binding ; Radiation counters ; Ribonucleoproteins - analysis ; Ribonucleoproteins - chemistry ; Ribonucleoproteins, Small Nuclear - metabolism ; RNA ; RNA Splicing ; RNA-Binding Proteins - analysis ; Sediments ; Small nuclear ribonucleoproteins ; Small nuclear RNA ; Spliceosomes ; Splicing ; Splicing Factor U2AF</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 1996-08, Vol.93 (17), p.8830-8835</ispartof><rights>Copyright 1996 National Academy of Sciences</rights><rights>Copyright National Academy of Sciences Aug 20, 1996</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c518t-a6c1861bf22c30f8d435833d761abf9d2361460425a3b0a860bf4d4ab01f18b63</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/93/17.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/39960$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/39960$$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/8799112$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yitzhaki, Shmuel</creatorcontrib><creatorcontrib>Miriami, Elana</creatorcontrib><creatorcontrib>Sperling, Ruth</creatorcontrib><creatorcontrib>Sperling, Joseph</creatorcontrib><title>Phosphorylated Ser/Arg-Rich Proteins: Limiting Factors in the Assembly of 200S Large Nuclear Ribonucleoprotein Particles</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>We have previously shown that specific nuclear pre-mRNA transcripts and their splicing products, as well as the general population of nuclear poly(A)+ RNA, are packaged in large nuclear ribonucleoprotein (lnRNP) particles that sediment at the 200S region in sucrose gradients. 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We further show that the structural integrity of lnRNP particles is sensitive to variations in the phosphorylation levels of the SR proteins.</description><subject>Animals</subject><subject>Aspartate Carbamoyltransferase - genetics</subject><subject>Cell Nucleus - metabolism</subject><subject>Cricetinae</subject><subject>Dihydroorotase - genetics</subject><subject>DNA-Binding Proteins - analysis</subject><subject>Gels</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Ligases - genetics</subject><subject>Nuclear Proteins - chemistry</subject><subject>Phosphoproteins - analysis</subject><subject>Phosphorylation</subject><subject>Polypyrimidine Tract-Binding Protein</subject><subject>Precipitin Tests</subject><subject>Protein Binding</subject><subject>Radiation counters</subject><subject>Ribonucleoproteins - analysis</subject><subject>Ribonucleoproteins - chemistry</subject><subject>Ribonucleoproteins, Small Nuclear - metabolism</subject><subject>RNA</subject><subject>RNA Splicing</subject><subject>RNA-Binding Proteins - analysis</subject><subject>Sediments</subject><subject>Small nuclear ribonucleoproteins</subject><subject>Small nuclear RNA</subject><subject>Spliceosomes</subject><subject>Splicing</subject><subject>Splicing Factor U2AF</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>eNqFks9v0zAcxS0EGt3gjIQEsjjAKe3XsePYiEs1MUCqoNrgbDmJ07hK48x20PrfL6GlYhzgZMvv855_PCP0gsCcQE4XfafDXNI5yedCUHiEZgQkSTiT8BjNANI8ESxlT9F5CFsAkJmAM3QmcikJSWfobt240DfO71sdTYVvjF8s_Sa5tmWD195FY7vwHq_szkbbbfCVLqPzAdsOx8bgZQhmV7R77GqcAtzglfYbg78OZWu0x9e2cN00d_0hCq-1j3ZcCM_Qk1q3wTw_jhfox9XH75efk9W3T18ul6ukzIiIieYlEZwUdZqWFGpRMZoJSqucE13UskopJ4wDSzNNC9CCQ1GziukCSE1EwekF-nDI7YdiZ6rSdNHrVvXe7rTfK6eteqh0tlEb91NRkWV0tL892r27HUyIamdDadpWd8YNQeWCZkRS8V-QZJwzkU-Jb_4Ct27w3fgGKgVCuWS_tl0coNK7ELypTwcmoKbi1VS8klSRXE3Fj45Xf97zxB-bHvXXR30y_lYfBLz7J6DqoW2juYsj-fJAbsP4F04olZIDvQe06suS</recordid><startdate>19960820</startdate><enddate>19960820</enddate><creator>Yitzhaki, Shmuel</creator><creator>Miriami, Elana</creator><creator>Sperling, Ruth</creator><creator>Sperling, Joseph</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>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>19960820</creationdate><title>Phosphorylated Ser/Arg-Rich Proteins: Limiting Factors in the Assembly of 200S Large Nuclear Ribonucleoprotein Particles</title><author>Yitzhaki, Shmuel ; Miriami, Elana ; Sperling, Ruth ; Sperling, Joseph</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c518t-a6c1861bf22c30f8d435833d761abf9d2361460425a3b0a860bf4d4ab01f18b63</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Animals</topic><topic>Aspartate Carbamoyltransferase - genetics</topic><topic>Cell Nucleus - metabolism</topic><topic>Cricetinae</topic><topic>Dihydroorotase - genetics</topic><topic>DNA-Binding Proteins - analysis</topic><topic>Gels</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>Ligases - genetics</topic><topic>Nuclear Proteins - chemistry</topic><topic>Phosphoproteins - analysis</topic><topic>Phosphorylation</topic><topic>Polypyrimidine Tract-Binding Protein</topic><topic>Precipitin Tests</topic><topic>Protein Binding</topic><topic>Radiation counters</topic><topic>Ribonucleoproteins - analysis</topic><topic>Ribonucleoproteins - chemistry</topic><topic>Ribonucleoproteins, Small Nuclear - metabolism</topic><topic>RNA</topic><topic>RNA Splicing</topic><topic>RNA-Binding Proteins - analysis</topic><topic>Sediments</topic><topic>Small nuclear ribonucleoproteins</topic><topic>Small nuclear RNA</topic><topic>Spliceosomes</topic><topic>Splicing</topic><topic>Splicing Factor U2AF</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yitzhaki, Shmuel</creatorcontrib><creatorcontrib>Miriami, Elana</creatorcontrib><creatorcontrib>Sperling, Ruth</creatorcontrib><creatorcontrib>Sperling, Joseph</creatorcontrib><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>MEDLINE - Academic</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>Yitzhaki, Shmuel</au><au>Miriami, Elana</au><au>Sperling, Ruth</au><au>Sperling, Joseph</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phosphorylated Ser/Arg-Rich Proteins: Limiting Factors in the Assembly of 200S Large Nuclear Ribonucleoprotein Particles</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>1996-08-20</date><risdate>1996</risdate><volume>93</volume><issue>17</issue><spage>8830</spage><epage>8835</epage><pages>8830-8835</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>We have previously shown that specific nuclear pre-mRNA transcripts and their splicing products, as well as the general population of nuclear poly(A)+ RNA, are packaged in large nuclear ribonucleoprotein (lnRNP) particles that sediment at the 200S region in sucrose gradients. 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| issn | 0027-8424 1091-6490 |
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| source | MEDLINE; Jstor Complete Legacy; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Animals Aspartate Carbamoyltransferase - genetics Cell Nucleus - metabolism Cricetinae Dihydroorotase - genetics DNA-Binding Proteins - analysis Gels HeLa Cells Humans Ligases - genetics Nuclear Proteins - chemistry Phosphoproteins - analysis Phosphorylation Polypyrimidine Tract-Binding Protein Precipitin Tests Protein Binding Radiation counters Ribonucleoproteins - analysis Ribonucleoproteins - chemistry Ribonucleoproteins, Small Nuclear - metabolism RNA RNA Splicing RNA-Binding Proteins - analysis Sediments Small nuclear ribonucleoproteins Small nuclear RNA Spliceosomes Splicing Splicing Factor U2AF |
| title | Phosphorylated Ser/Arg-Rich Proteins: Limiting Factors in the Assembly of 200S Large Nuclear Ribonucleoprotein Particles |
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