Association of yeast RNA polymerase I with a nucleolar substructure active in rRNA synthesis and processing
A novel ribonucleoprotein complex enriched in nucleolar proteins was purified from yeast extracts and constituents were identified by mass spectrometry. When isolated from rapidly growing cells, the assembly contained ribonucleic acid (RNA) polymerase (pol) I, and some of its transcription factors l...
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| Veröffentlicht in: | The Journal of cell biology 2000-05, Vol.149 (3), p.575-589 |
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| container_title | The Journal of cell biology |
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| creator | Fath, S Milkereit, P Podtelejnikov, A.V Bischler, N Schultz, P Bier, M Mann, M Tschochner, H |
| description | A novel ribonucleoprotein complex enriched in nucleolar proteins was purified from yeast extracts and constituents were identified by mass spectrometry. When isolated from rapidly growing cells, the assembly contained ribonucleic acid (RNA) polymerase (pol) I, and some of its transcription factors like TATA-binding protein (TBP), Rrn3p, Rrn5p, Rrn7p, and Reb1p along with rRNA processing factors, like Nop1p, Cbf5p, Nhp2p, and Rrp5p. The small nucleolar RNAs (snoRNAs) U3, U14, and MRP were also found to be associated with the complex, which supports accurate transcription, termination, and pseudouridylation of rRNA. Formation of the complex did not depend on pol I, and the complex could efficiently recruit exogenous pol I into active ribosomal DNA (rDNA) transcription units. Visualization of the complex by electron microscopy and immunogold labeling revealed a characteristic cluster-forming network of nonuniform size containing nucleolar proteins like Nop1p and Fpr3p and attached pol I. Our results support the idea that a functional nucleolar subdomain formed independently of the state of rDNA transcription may serve as a scaf-fold for coordinated rRNA synthesis and processing. |
| doi_str_mv | 10.1083/jcb.149.3.575 |
| format | Article |
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When isolated from rapidly growing cells, the assembly contained ribonucleic acid (RNA) polymerase (pol) I, and some of its transcription factors like TATA-binding protein (TBP), Rrn3p, Rrn5p, Rrn7p, and Reb1p along with rRNA processing factors, like Nop1p, Cbf5p, Nhp2p, and Rrp5p. The small nucleolar RNAs (snoRNAs) U3, U14, and MRP were also found to be associated with the complex, which supports accurate transcription, termination, and pseudouridylation of rRNA. Formation of the complex did not depend on pol I, and the complex could efficiently recruit exogenous pol I into active ribosomal DNA (rDNA) transcription units. Visualization of the complex by electron microscopy and immunogold labeling revealed a characteristic cluster-forming network of nonuniform size containing nucleolar proteins like Nop1p and Fpr3p and attached pol I. Our results support the idea that a functional nucleolar subdomain formed independently of the state of rDNA transcription may serve as a scaf-fold for coordinated rRNA synthesis and processing.</description><identifier>ISSN: 0021-9525</identifier><identifier>EISSN: 1540-8140</identifier><identifier>DOI: 10.1083/jcb.149.3.575</identifier><identifier>PMID: 10791972</identifier><identifier>CODEN: JCLBA3</identifier><language>eng</language><publisher>United States: Rockefeller University Press</publisher><subject>Antibodies ; binding proteins ; Cbf5 protein ; Cell nucleolus ; Cell Nucleolus - metabolism ; Cells ; Cellular Biology ; DNA, Ribosomal - genetics ; DNA-directed RNA polymerase ; Fpr3 protein ; Gels ; Genes ; Life Sciences ; Macromolecular Substances ; Mass Spectrometry ; Microscopy, Immunoelectron ; MRP protein ; Nhp2 protein ; Nop1 protein ; Nuclear proteins ; Nuclear Proteins - chemistry ; nucleolar proteins ; Original ; Proteins ; Reb1 protein ; Ribonucleic acid ; Ribonucleoproteins - chemistry ; Ribosomal DNA ; ribosomal RNA ; ribosomal rna processing factors ; ribosomes ; RNA ; RNA Polymerase I - genetics ; RNA Polymerase I - metabolism ; RNA, Ribosomal - biosynthesis ; RNA, Ribosomal - metabolism ; RNA, Small Nucleolar - chemistry ; Rrn3 protein ; Rrn7 protein ; rRNA ; Rrp5 protein ; Saccharomyces cerevisiae ; Small nucleolar RNA ; snoRNA U14 ; snoRNA U3 ; transcription (genetics) ; transcription factors ; Transcription Factors - chemistry ; Transcription, Genetic ; Yeast ; Yeasts</subject><ispartof>The Journal of cell biology, 2000-05, Vol.149 (3), p.575-589</ispartof><rights>Copyright 2000 The Rockefeller University Press</rights><rights>Copyright Rockefeller University Press May 1, 2000</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><rights>2000 The Rockefeller University Press 2000 The Rockefeller University Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c520t-ccaa80c5fba7d9d0f97388b74d86c38a44427ca983403e8d73709fc008bc0c63</citedby><cites>FETCH-LOGICAL-c520t-ccaa80c5fba7d9d0f97388b74d86c38a44427ca983403e8d73709fc008bc0c63</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/10791972$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://hal.science/hal-04094313$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Fath, S</creatorcontrib><creatorcontrib>Milkereit, P</creatorcontrib><creatorcontrib>Podtelejnikov, A.V</creatorcontrib><creatorcontrib>Bischler, N</creatorcontrib><creatorcontrib>Schultz, P</creatorcontrib><creatorcontrib>Bier, M</creatorcontrib><creatorcontrib>Mann, M</creatorcontrib><creatorcontrib>Tschochner, H</creatorcontrib><title>Association of yeast RNA polymerase I with a nucleolar substructure active in rRNA synthesis and processing</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>A novel ribonucleoprotein complex enriched in nucleolar proteins was purified from yeast extracts and constituents were identified by mass spectrometry. When isolated from rapidly growing cells, the assembly contained ribonucleic acid (RNA) polymerase (pol) I, and some of its transcription factors like TATA-binding protein (TBP), Rrn3p, Rrn5p, Rrn7p, and Reb1p along with rRNA processing factors, like Nop1p, Cbf5p, Nhp2p, and Rrp5p. The small nucleolar RNAs (snoRNAs) U3, U14, and MRP were also found to be associated with the complex, which supports accurate transcription, termination, and pseudouridylation of rRNA. Formation of the complex did not depend on pol I, and the complex could efficiently recruit exogenous pol I into active ribosomal DNA (rDNA) transcription units. Visualization of the complex by electron microscopy and immunogold labeling revealed a characteristic cluster-forming network of nonuniform size containing nucleolar proteins like Nop1p and Fpr3p and attached pol I. Our results support the idea that a functional nucleolar subdomain formed independently of the state of rDNA transcription may serve as a scaf-fold for coordinated rRNA synthesis and processing.</description><subject>Antibodies</subject><subject>binding proteins</subject><subject>Cbf5 protein</subject><subject>Cell nucleolus</subject><subject>Cell Nucleolus - metabolism</subject><subject>Cells</subject><subject>Cellular Biology</subject><subject>DNA, Ribosomal - genetics</subject><subject>DNA-directed RNA polymerase</subject><subject>Fpr3 protein</subject><subject>Gels</subject><subject>Genes</subject><subject>Life Sciences</subject><subject>Macromolecular Substances</subject><subject>Mass Spectrometry</subject><subject>Microscopy, Immunoelectron</subject><subject>MRP protein</subject><subject>Nhp2 protein</subject><subject>Nop1 protein</subject><subject>Nuclear proteins</subject><subject>Nuclear Proteins - chemistry</subject><subject>nucleolar proteins</subject><subject>Original</subject><subject>Proteins</subject><subject>Reb1 protein</subject><subject>Ribonucleic acid</subject><subject>Ribonucleoproteins - chemistry</subject><subject>Ribosomal DNA</subject><subject>ribosomal RNA</subject><subject>ribosomal rna processing factors</subject><subject>ribosomes</subject><subject>RNA</subject><subject>RNA Polymerase I - genetics</subject><subject>RNA Polymerase I - metabolism</subject><subject>RNA, Ribosomal - biosynthesis</subject><subject>RNA, Ribosomal - metabolism</subject><subject>RNA, Small Nucleolar - chemistry</subject><subject>Rrn3 protein</subject><subject>Rrn7 protein</subject><subject>rRNA</subject><subject>Rrp5 protein</subject><subject>Saccharomyces cerevisiae</subject><subject>Small nucleolar RNA</subject><subject>snoRNA U14</subject><subject>snoRNA U3</subject><subject>transcription (genetics)</subject><subject>transcription factors</subject><subject>Transcription Factors - chemistry</subject><subject>Transcription, Genetic</subject><subject>Yeast</subject><subject>Yeasts</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFksGLEzEUxgdR3O7q0Zto8CB4mPoyyTTJRSjL6i4UBV3PIZPJtKnTSc3LVPrfmzKLrnvxFMj3e19ePr6ieEFhTkGy91vbzClXczavRf2omNGaQykph8fFDKCipaqr-qw4R9wCABecPS3OKAhFlahmxY8lYrDeJB8GEjpydAYT-fp5SfahP-5cNOjIDfnl04YYMoy2d6E3keDYYIqjTWN0xNjkD474gcTTJB6HtHHokZihJfsYrEP0w_pZ8aQzPbrnd-dFcfvx6vbyulx9-XRzuVyVtq4gldYaI8HWXWNEq1rolGBSNoK3cmGZNJzzSlijJOPAnGwFE6A6CyAbC3bBLooPk-1-bHautW5I0fR6H_3OxKMOxut_lcFv9DocdEUFlwvIBu8mg82DsevlSp_ugIPijLIDzezbu8di-Dk6THrn0bq-N4MLI2qRo64Flf8FqagZl-IEvnkAbsMYhxzYaUHIv61ZhsoJsjEgRtf92ZOCPvVC517o3AvNdO5F5l_dz-QePRUhAy8nYIspxL_6IqucZ_n1JHcmaLOOHvX3bxVQBpXiSi4q9huv5cbW</recordid><startdate>20000501</startdate><enddate>20000501</enddate><creator>Fath, S</creator><creator>Milkereit, P</creator><creator>Podtelejnikov, A.V</creator><creator>Bischler, N</creator><creator>Schultz, P</creator><creator>Bier, M</creator><creator>Mann, M</creator><creator>Tschochner, H</creator><general>Rockefeller University Press</general><general>The Rockefeller University Press</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>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7TM</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>1XC</scope><scope>5PM</scope></search><sort><creationdate>20000501</creationdate><title>Association of yeast RNA polymerase I with a nucleolar substructure active in rRNA synthesis and processing</title><author>Fath, S ; 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When isolated from rapidly growing cells, the assembly contained ribonucleic acid (RNA) polymerase (pol) I, and some of its transcription factors like TATA-binding protein (TBP), Rrn3p, Rrn5p, Rrn7p, and Reb1p along with rRNA processing factors, like Nop1p, Cbf5p, Nhp2p, and Rrp5p. The small nucleolar RNAs (snoRNAs) U3, U14, and MRP were also found to be associated with the complex, which supports accurate transcription, termination, and pseudouridylation of rRNA. Formation of the complex did not depend on pol I, and the complex could efficiently recruit exogenous pol I into active ribosomal DNA (rDNA) transcription units. Visualization of the complex by electron microscopy and immunogold labeling revealed a characteristic cluster-forming network of nonuniform size containing nucleolar proteins like Nop1p and Fpr3p and attached pol I. Our results support the idea that a functional nucleolar subdomain formed independently of the state of rDNA transcription may serve as a scaf-fold for coordinated rRNA synthesis and processing.</abstract><cop>United States</cop><pub>Rockefeller University Press</pub><pmid>10791972</pmid><doi>10.1083/jcb.149.3.575</doi><tpages>15</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Antibodies binding proteins Cbf5 protein Cell nucleolus Cell Nucleolus - metabolism Cells Cellular Biology DNA, Ribosomal - genetics DNA-directed RNA polymerase Fpr3 protein Gels Genes Life Sciences Macromolecular Substances Mass Spectrometry Microscopy, Immunoelectron MRP protein Nhp2 protein Nop1 protein Nuclear proteins Nuclear Proteins - chemistry nucleolar proteins Original Proteins Reb1 protein Ribonucleic acid Ribonucleoproteins - chemistry Ribosomal DNA ribosomal RNA ribosomal rna processing factors ribosomes RNA RNA Polymerase I - genetics RNA Polymerase I - metabolism RNA, Ribosomal - biosynthesis RNA, Ribosomal - metabolism RNA, Small Nucleolar - chemistry Rrn3 protein Rrn7 protein rRNA Rrp5 protein Saccharomyces cerevisiae Small nucleolar RNA snoRNA U14 snoRNA U3 transcription (genetics) transcription factors Transcription Factors - chemistry Transcription, Genetic Yeast Yeasts |
| title | Association of yeast RNA polymerase I with a nucleolar substructure active in rRNA synthesis and processing |
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