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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
13
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pubmed:dateCreated |
2009-7-9
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pubmed:abstractText |
Eukaryotic DNA replication requires the coordinated activity of the multi-subunit DNA polymerases: Pol alpha, Pol delta and Pol epsilon. The conserved catalytic and regulatory B subunits associate in a constitutive heterodimer that represents the functional core of all three replicative polymerases. Here, we combine X-ray crystallography and electron microscopy (EM) to describe subunit interaction and 3D architecture of heterodimeric yeast Pol alpha. The crystal structure of the C-terminal domain (CTD) of the catalytic subunit bound to the B subunit illustrates a conserved mechanism of accessory factor recruitment by replicative polymerases. The EM reconstructions of Pol alpha reveal a bilobal shape with separate catalytic and regulatory modules. Docking of the B-CTD complex in the EM reconstruction shows that the B subunit is tethered to the polymerase domain through a structured but flexible linker. Our combined findings provide a structural template for the common functional architecture of the three major replicative DNA polymerases.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-10087916,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-10089348,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-10360184,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-10428796,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-10523676,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-10600563,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-10829230,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-11416129,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-11472087,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-12781660,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-14499601,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-15046581,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-15173383,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-15299926,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-15477099,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-15568020,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-15572765,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-15808859,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-15980475,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-16369485,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-16963278,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-17150992,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-17179934,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-18157155,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-18340343,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-18471969,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-18542881,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-18614176,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-18818516,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-2169349,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-7813016,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-7823954,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-8417347,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-9258670,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-9356477,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-9685491,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-9792727,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-9826686,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19494830-9918845
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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 |
Jul
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pubmed:issn |
1460-2075
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
8
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pubmed:volume |
28
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1978-87
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pubmed:dateRevised |
2010-4-26
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pubmed:meshHeading |
pubmed-meshheading:19494830-Amino Acid Sequence,
pubmed-meshheading:19494830-Animals,
pubmed-meshheading:19494830-Crystallography, X-Ray,
pubmed-meshheading:19494830-DNA Polymerase I,
pubmed-meshheading:19494830-Escherichia coli,
pubmed-meshheading:19494830-Humans,
pubmed-meshheading:19494830-Microscopy, Electron,
pubmed-meshheading:19494830-Models, Molecular,
pubmed-meshheading:19494830-Molecular Sequence Data,
pubmed-meshheading:19494830-Protein Conformation,
pubmed-meshheading:19494830-Protein Structure, Tertiary,
pubmed-meshheading:19494830-Protein Subunits,
pubmed-meshheading:19494830-Saccharomyces cerevisiae,
pubmed-meshheading:19494830-Sequence Alignment
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pubmed:year |
2009
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pubmed:articleTitle |
3D architecture of DNA Pol alpha reveals the functional core of multi-subunit replicative polymerases.
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pubmed:affiliation |
Department of Biochemistry, University of Cambridge, Cambridge, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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