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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...

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Autores principales: Fath, Stephan, Milkereit, Philipp, Podtelejnikov, Alexandre V., Bischler, Nicolas, Schultz, Patrick, Bier, Mirko, Mann, Matthias, Tschochner, Herbert
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2000
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.
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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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