| pubmed-article:7634403 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7634403 | lifeskim:mentions | umls-concept:C0598312 | lld:lifeskim |
| pubmed-article:7634403 | lifeskim:mentions | umls-concept:C1533157 | lld:lifeskim |
| pubmed-article:7634403 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:7634403 | pubmed:dateCreated | 1995-9-14 | lld:pubmed |
| pubmed-article:7634403 | pubmed:abstractText | The ability of Klenow polymerase I, phage T7 polymerase (Sequenase), human polymerase alpha, and human polymerase beta to synthesize past (bypass) O6-methylguanine (O6-meG) lesions was studied in the presence of MgCl2 and MnCl2. An end-labeled 16-mer primer was annealed to the 3' end of gel-purified oligodeoxyribonucleotide templates (45-mers), each containing a single O6-meG in place of one G in the sequence -G1G2CG3G4T-. Extension products were analyzed by denaturing polyacrylamide gel electrophoresis and autoradiography. A fraction of the products extended by Klenow fragment terminated either opposite or one base before O6-meG located at sites 1 and 3. Termination occurred primarily one base before O6-meG located at sites 2 and 4. The remaining fractions that bypassed the lesions represented full-length product. In control reactions, the O6-meG-containing templates were annealed with complementary 45-mers, repaired with O6-alkylguanine DNA-alkyltransferase, annealed with an excess of labeled primer, and extended by Klenow fragment. Full-length extension of > 90% was observed with each template. Primer extension past O6-meG by DNA polymerase alpha and Sequenase was partially blocked in a manner which varied with the site of O6-meG in the template while primer extension by DNA polymerase beta was completely blocked (< 2% full length extension) with O6-meG at sites 1-4. Substitution of MnCl2 for MgCl2 in the reaction mixture greatly increased the bypass of O6-meG by Klenow fragment and DNA polymerase alpha but not Sequenase or DNA polymerase beta. The increased ability of Klenow fragment to bypass O6-meG in the presence of MnCl2 was found to result from an increased incorporation of G (O6-meG at sites 1 and 2) and A (O6-meG at sites 1, 2, and 3) opposite the lesion. The results indicate that O6-meG can block in vitro polymerization by several DNA polymerases and are consistent with the observed cytotoxic effects of methylating agents on mammalian cells. | lld:pubmed |
| pubmed-article:7634403 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7634403 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7634403 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7634403 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7634403 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7634403 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7634403 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7634403 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7634403 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7634403 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:7634403 | pubmed:issn | 0143-3334 | lld:pubmed |
| pubmed-article:7634403 | pubmed:author | pubmed-author:TopalM DMD | lld:pubmed |
| pubmed-article:7634403 | pubmed:author | pubmed-author:VoigtJ MJM | lld:pubmed |
| pubmed-article:7634403 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7634403 | pubmed:volume | 16 | lld:pubmed |
| pubmed-article:7634403 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7634403 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7634403 | pubmed:pagination | 1775-82 | lld:pubmed |
| pubmed-article:7634403 | pubmed:dateRevised | 2004-11-17 | lld:pubmed |
| pubmed-article:7634403 | pubmed:meshHeading | pubmed-meshheading:7634403-... | lld:pubmed |
| pubmed-article:7634403 | pubmed:meshHeading | pubmed-meshheading:7634403-... | lld:pubmed |
| pubmed-article:7634403 | pubmed:meshHeading | pubmed-meshheading:7634403-... | lld:pubmed |
| pubmed-article:7634403 | pubmed:meshHeading | pubmed-meshheading:7634403-... | lld:pubmed |
| pubmed-article:7634403 | pubmed:meshHeading | pubmed-meshheading:7634403-... | lld:pubmed |
| pubmed-article:7634403 | pubmed:meshHeading | pubmed-meshheading:7634403-... | lld:pubmed |
| pubmed-article:7634403 | pubmed:meshHeading | pubmed-meshheading:7634403-... | lld:pubmed |
| pubmed-article:7634403 | pubmed:meshHeading | pubmed-meshheading:7634403-... | lld:pubmed |
| pubmed-article:7634403 | pubmed:meshHeading | pubmed-meshheading:7634403-... | lld:pubmed |
| pubmed-article:7634403 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7634403 | pubmed:articleTitle | O6-methylguanine-induced replication blocks. | lld:pubmed |
| pubmed-article:7634403 | pubmed:affiliation | Department of Pharmacology and Toxicology, Philadelphia College of Pharmacy and Science, PA 19104, USA. | lld:pubmed |
| pubmed-article:7634403 | pubmed:publicationType | Journal Article | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:7634403 | lld:pubmed |
