rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2011-1-11
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pubmed:abstractText |
RNA polymerases are essential enzymes which transcribe DNA into RNA. Here, we obtain mass spectra of the cellular forms of apo and holo eukaryotic RNA polymerase I and III, defining their composition under different solution conditions. By recombinant expression of subunits within the initiation heterotrimer of Pol III, we derive an interaction network and couple this data with ion mobility data to define topological restraints. Our data agree with available structural information and homology modeling and are generally consistent with yeast two hybrid data. Unexpectedly, elongation complexes of both Pol I and III destabilize the assemblies compared with their apo counterparts. Increasing the pH and ionic strength of apo and holo forms of Pol I and Pol III leads to formation of at least ten stable subcomplexes for both enzymes. Uniquely for Pol III many subcomplexes contain only one of the two largest catalytic subunits. We speculate that these stable subcomplexes represent putative intermediates in assembly pathways.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1878-4186
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pubmed:author |
pubmed-author:Fernández-TorneroCarlosC,
pubmed-author:GavinAnne-ClaudeAC,
pubmed-author:GvozdenovicJelenaJ,
pubmed-author:LaneLaura ALA,
pubmed-author:LindnerDorisD,
pubmed-author:MüllerChristoph WCW,
pubmed-author:MorgnerNinaN,
pubmed-author:PolitisArgyrisA,
pubmed-author:PtchelkineDenisD,
pubmed-author:RobinsonCarol VCV,
pubmed-author:SteuerwaldUlrichU,
pubmed-author:ZhouMinM
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pubmed:copyrightInfo |
Copyright © 2011 Elsevier Ltd. All rights reserved.
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pubmed:issnType |
Electronic
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pubmed:day |
12
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pubmed:volume |
19
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
90-100
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pubmed:meshHeading |
pubmed-meshheading:21220119-Apoenzymes,
pubmed-meshheading:21220119-Polydeoxyribonucleotides,
pubmed-meshheading:21220119-Protein Multimerization,
pubmed-meshheading:21220119-Protein Stability,
pubmed-meshheading:21220119-Protein Structure, Quaternary,
pubmed-meshheading:21220119-Protein Structure, Tertiary,
pubmed-meshheading:21220119-RNA Polymerase I,
pubmed-meshheading:21220119-RNA Polymerase III,
pubmed-meshheading:21220119-Saccharomyces cerevisiae,
pubmed-meshheading:21220119-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:21220119-Spectrometry, Mass, Electrospray Ionization
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pubmed:year |
2011
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pubmed:articleTitle |
Mass spectrometry reveals stable modules in holo and apo RNA polymerases I and III.
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pubmed:affiliation |
Department of Chemistry, Chemistry Research Laboratory, Mansfield Road, Oxford OX1 3TA, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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