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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...
Autores principales: | , , , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2000
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2174860/ https://www.ncbi.nlm.nih.gov/pubmed/10791972 |
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author | Fath, Stephan Milkereit, Philipp Podtelejnikov, Alexandre V. Bischler, Nicolas Schultz, Patrick Bier, Mirko Mann, Matthias Tschochner, Herbert |
author_facet | Fath, Stephan Milkereit, Philipp Podtelejnikov, Alexandre V. Bischler, Nicolas Schultz, Patrick Bier, Mirko Mann, Matthias Tschochner, Herbert |
author_sort | Fath, Stephan |
collection | PubMed |
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 scaffold for coordinated rRNA synthesis and processing. |
format | Text |
id | pubmed-2174860 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2000 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21748602008-05-01 Association of Yeast RNA Polymerase I with a Nucleolar Substructure Active in Rrna Synthesis and Processing Fath, Stephan Milkereit, Philipp Podtelejnikov, Alexandre V. Bischler, Nicolas Schultz, Patrick Bier, Mirko Mann, Matthias Tschochner, Herbert J Cell Biol Original Article 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 scaffold for coordinated rRNA synthesis and processing. The Rockefeller University Press 2000-05-01 /pmc/articles/PMC2174860/ /pubmed/10791972 Text en © 2000 The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Original Article Fath, Stephan Milkereit, Philipp Podtelejnikov, Alexandre V. Bischler, Nicolas Schultz, Patrick Bier, Mirko Mann, Matthias Tschochner, Herbert Association of Yeast RNA Polymerase I with a Nucleolar Substructure Active in Rrna Synthesis and Processing |
title | Association of Yeast RNA Polymerase I with a Nucleolar Substructure Active in Rrna Synthesis and Processing |
title_full | Association of Yeast RNA Polymerase I with a Nucleolar Substructure Active in Rrna Synthesis and Processing |
title_fullStr | Association of Yeast RNA Polymerase I with a Nucleolar Substructure Active in Rrna Synthesis and Processing |
title_full_unstemmed | Association of Yeast RNA Polymerase I with a Nucleolar Substructure Active in Rrna Synthesis and Processing |
title_short | Association of Yeast RNA Polymerase I with a Nucleolar Substructure Active in Rrna Synthesis and Processing |
title_sort | association of yeast rna polymerase i with a nucleolar substructure active in rrna synthesis and processing |
topic | Original Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2174860/ https://www.ncbi.nlm.nih.gov/pubmed/10791972 |
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