| pubmed-article:12899630 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12899630 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
| pubmed-article:12899630 | lifeskim:mentions | umls-concept:C0205681 | lld:lifeskim |
| pubmed-article:12899630 | lifeskim:mentions | umls-concept:C1948035 | lld:lifeskim |
| pubmed-article:12899630 | lifeskim:mentions | umls-concept:C1553387 | lld:lifeskim |
| pubmed-article:12899630 | lifeskim:mentions | umls-concept:C1521805 | lld:lifeskim |
| pubmed-article:12899630 | lifeskim:mentions | umls-concept:C1720127 | lld:lifeskim |
| pubmed-article:12899630 | lifeskim:mentions | umls-concept:C0596448 | lld:lifeskim |
| pubmed-article:12899630 | lifeskim:mentions | umls-concept:C0040092 | lld:lifeskim |
| pubmed-article:12899630 | pubmed:issue | 31 | lld:pubmed |
| pubmed-article:12899630 | pubmed:dateCreated | 2003-8-5 | lld:pubmed |
| pubmed-article:12899630 | pubmed:abstractText | Polymerase eta is a member of the Y family of DNA polymerases which is able to bypass thymine dimers efficiently and in a relatively error-free manner. To elucidate the mechanism of dimer bypass, the efficiency of dAMP and pyrene nucleotide insertion opposite the thymine dimer and its N3-methyl derivatives was determined. Pol eta inserts pyrene nucleotide with greater efficiency than dAMP opposite the 3'-T of an undimerized or dimerized T and is an effective inhibitor of DNA synthesis by pol eta. Substitution of the N3H of the 3'-T of an undimerized T or a dimerized T with a methyl group has little effect on the insertion efficiency of pyrene nucleotide but greatly inhibits the insertion of dAMP. Together, these results suggest that the error-free insertion of dAMP opposite the 3'-T of the cis-syn thymine dimer happens by way of a loosely held dimer in the active site which can be displaced from the active site by pyrene nucleotide. In contrast, pol eta cannot insert pyrene nucleotide opposite the 5'-T of the dimer, whereas it can insert dAMP with efficiency comparable to that opposite the 3'-T. The inability to insert pyrene nucleotide opposite the 5'-T of the dimer is consistent with the idea that while the polymerase binds loosely to a templating nucleotide, it binds tightly to the nucleotide to its 3'-side. Overall, the results show a marked difference from similar studies on pol I family polymerases, and suggest mechanisms by which this Y family polymerase can process damaged DNA efficiently. | lld:pubmed |
| pubmed-article:12899630 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12899630 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12899630 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12899630 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12899630 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12899630 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12899630 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12899630 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12899630 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12899630 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12899630 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12899630 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12899630 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:12899630 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:12899630 | pubmed:author | pubmed-author:DohanichG PGP | lld:pubmed |
| pubmed-article:12899630 | pubmed:author | pubmed-author:KoolEric TET | lld:pubmed |
| pubmed-article:12899630 | pubmed:author | pubmed-author:WangZhigangZ | lld:pubmed |
| pubmed-article:12899630 | pubmed:author | pubmed-author:SunLipingL | lld:pubmed |
| pubmed-article:12899630 | pubmed:author | pubmed-author:ZhangKaijiang... | lld:pubmed |
| pubmed-article:12899630 | pubmed:author | pubmed-author:ZhouLillyL | lld:pubmed |
| pubmed-article:12899630 | pubmed:author | pubmed-author:HohlerPaulP | lld:pubmed |
| pubmed-article:12899630 | pubmed:author | pubmed-author:YuanFenghuaF | lld:pubmed |
| pubmed-article:12899630 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12899630 | pubmed:day | 12 | lld:pubmed |
| pubmed-article:12899630 | pubmed:volume | 42 | lld:pubmed |
| pubmed-article:12899630 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12899630 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12899630 | pubmed:pagination | 9431-7 | lld:pubmed |
| pubmed-article:12899630 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:12899630 | pubmed:meshHeading | pubmed-meshheading:12899630... | lld:pubmed |
| pubmed-article:12899630 | pubmed:meshHeading | pubmed-meshheading:12899630... | lld:pubmed |
| pubmed-article:12899630 | pubmed:meshHeading | pubmed-meshheading:12899630... | lld:pubmed |
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| pubmed-article:12899630 | pubmed:meshHeading | pubmed-meshheading:12899630... | lld:pubmed |
| pubmed-article:12899630 | pubmed:meshHeading | pubmed-meshheading:12899630... | lld:pubmed |
| pubmed-article:12899630 | pubmed:meshHeading | pubmed-meshheading:12899630... | lld:pubmed |
| pubmed-article:12899630 | pubmed:meshHeading | pubmed-meshheading:12899630... | lld:pubmed |
| pubmed-article:12899630 | pubmed:meshHeading | pubmed-meshheading:12899630... | lld:pubmed |
| pubmed-article:12899630 | pubmed:meshHeading | pubmed-meshheading:12899630... | lld:pubmed |
| pubmed-article:12899630 | pubmed:meshHeading | pubmed-meshheading:12899630... | lld:pubmed |
| pubmed-article:12899630 | pubmed:meshHeading | pubmed-meshheading:12899630... | lld:pubmed |
| pubmed-article:12899630 | pubmed:meshHeading | pubmed-meshheading:12899630... | lld:pubmed |
| pubmed-article:12899630 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12899630 | pubmed:articleTitle | Yeast pol eta holds a cis-syn thymine dimer loosely in the active site during elongation opposite the 3'-T of the dimer, but tightly opposite the 5'-T. | lld:pubmed |
| pubmed-article:12899630 | pubmed:affiliation | Department of Chemistry, Washington University, St. Louis, Missouri 63130, USA. | lld:pubmed |
| pubmed-article:12899630 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12899630 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:12899630 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:12899630 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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