| pubmed-article:19494830 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19494830 | lifeskim:mentions | umls-concept:C0012854 | lld:lifeskim |
| pubmed-article:19494830 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:19494830 | lifeskim:mentions | umls-concept:C1335439 | lld:lifeskim |
| pubmed-article:19494830 | lifeskim:mentions | umls-concept:C2003941 | lld:lifeskim |
| pubmed-article:19494830 | lifeskim:mentions | umls-concept:C0444669 | lld:lifeskim |
| pubmed-article:19494830 | lifeskim:mentions | umls-concept:C0003737 | lld:lifeskim |
| pubmed-article:19494830 | pubmed:issue | 13 | lld:pubmed |
| pubmed-article:19494830 | pubmed:dateCreated | 2009-7-9 | lld:pubmed |
| pubmed-article:19494830 | 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. | lld:pubmed |
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| pubmed-article:19494830 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19494830 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19494830 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:19494830 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19494830 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:19494830 | pubmed:issn | 1460-2075 | lld:pubmed |
| pubmed-article:19494830 | pubmed:author | pubmed-author:PellegriniLuc... | lld:pubmed |
| pubmed-article:19494830 | pubmed:author | pubmed-author:LlorcaOscarO | lld:pubmed |
| pubmed-article:19494830 | pubmed:author | pubmed-author:Núñez-Ramírez... | lld:pubmed |
| pubmed-article:19494830 | pubmed:author | pubmed-author:KlingeSebasti... | lld:pubmed |
| pubmed-article:19494830 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19494830 | pubmed:day | 8 | lld:pubmed |
| pubmed-article:19494830 | pubmed:volume | 28 | lld:pubmed |
| pubmed-article:19494830 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19494830 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19494830 | pubmed:pagination | 1978-87 | lld:pubmed |
| pubmed-article:19494830 | pubmed:dateRevised | 2010-4-26 | lld:pubmed |
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| pubmed-article:19494830 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19494830 | pubmed:articleTitle | 3D architecture of DNA Pol alpha reveals the functional core of multi-subunit replicative polymerases. | lld:pubmed |
| pubmed-article:19494830 | pubmed:affiliation | Department of Biochemistry, University of Cambridge, Cambridge, UK. | lld:pubmed |
| pubmed-article:19494830 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19494830 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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