| pubmed-article:11772403 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11772403 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:11772403 | lifeskim:mentions | umls-concept:C0012854 | lld:lifeskim |
| pubmed-article:11772403 | lifeskim:mentions | umls-concept:C0525039 | lld:lifeskim |
| pubmed-article:11772403 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:11772403 | lifeskim:mentions | umls-concept:C0600364 | lld:lifeskim |
| pubmed-article:11772403 | lifeskim:mentions | umls-concept:C2603343 | lld:lifeskim |
| pubmed-article:11772403 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
| pubmed-article:11772403 | lifeskim:mentions | umls-concept:C1513371 | lld:lifeskim |
| pubmed-article:11772403 | pubmed:issue | Pt 2 | lld:pubmed |
| pubmed-article:11772403 | pubmed:dateCreated | 2002-1-4 | lld:pubmed |
| pubmed-article:11772403 | pubmed:abstractText | The interaction of a series of DNA substrates with human DNA polymerase beta has been studied in real time by using a surface-plasmon-resonance (SPR) biosensor technique. We have prepared the sensor surfaces comprising different DNA targets, including single-stranded DNA, blunt-end double-stranded DNA, gapped DNA and DNA template-primer duplexes containing various mismatches at different positions. The binding and dissociation of polymerase beta at the DNA-modified surfaces was measured in real time, and the kinetics profiles of polymerase-DNA interaction were analysed using various physical models. The results showed that polymerase beta binding to single-stranded DNA (K(A)=1.25 x 10(8) M(-1); where K(A) is the equilibrium affinity constant) was thermodynamically more favourable than to blunt-end DNA duplex (K(A)=7.56x10(7) M(-1)) or gapped DNA (K(A)=8.53x10(7) M(-1)), with a single binding mode on each DNA substrate. However, polymerase beta bound to DNA template-primer duplexes (15 bp with a 35 nt overhang) at two sites, presumably one at the single-strand overhang and the other at the 3'-end of the primer. When the DNA duplex was fully matched, most of the polymerase beta (83%) bound to the template-primer duplex region. The introduction of different numbers of mismatches near the 3'-end of the primer caused the binding affinity and the fraction of polymerase beta bound at the duplex region to decrease 8-58-fold and 15-40%, respectively. On the other hand, the affinity of polymerase beta for the single-strand overhang remained unchanged while the fraction bound to the single-strand region increased by 15-40%. The destabilizing effect of the mismatches was due to both a decrease in the rate of binding and an increase in the rate of dissociation for polymerase beta. | lld:pubmed |
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| pubmed-article:11772403 | pubmed:language | eng | lld:pubmed |
| pubmed-article:11772403 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11772403 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11772403 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11772403 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11772403 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11772403 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:11772403 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:11772403 | pubmed:author | pubmed-author:TsoiPui YanPY | lld:pubmed |
| pubmed-article:11772403 | pubmed:author | pubmed-author:YangMengsuM | lld:pubmed |
| pubmed-article:11772403 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11772403 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:11772403 | pubmed:volume | 361 | lld:pubmed |
| pubmed-article:11772403 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11772403 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11772403 | pubmed:pagination | 317-25 | lld:pubmed |
| pubmed-article:11772403 | pubmed:dateRevised | 2010-9-14 | lld:pubmed |
| pubmed-article:11772403 | pubmed:meshHeading | pubmed-meshheading:11772403... | lld:pubmed |
| pubmed-article:11772403 | pubmed:meshHeading | pubmed-meshheading:11772403... | lld:pubmed |
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| pubmed-article:11772403 | pubmed:meshHeading | pubmed-meshheading:11772403... | lld:pubmed |
| pubmed-article:11772403 | pubmed:meshHeading | pubmed-meshheading:11772403... | lld:pubmed |
| pubmed-article:11772403 | pubmed:meshHeading | pubmed-meshheading:11772403... | lld:pubmed |
| pubmed-article:11772403 | pubmed:meshHeading | pubmed-meshheading:11772403... | lld:pubmed |
| pubmed-article:11772403 | pubmed:meshHeading | pubmed-meshheading:11772403... | lld:pubmed |
| pubmed-article:11772403 | pubmed:meshHeading | pubmed-meshheading:11772403... | lld:pubmed |
| pubmed-article:11772403 | pubmed:meshHeading | pubmed-meshheading:11772403... | lld:pubmed |
| pubmed-article:11772403 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:11772403 | pubmed:articleTitle | Kinetic study of various binding modes between human DNA polymerase beta and different DNA substrates by surface-plasmon-resonance biosensor. | lld:pubmed |
| pubmed-article:11772403 | pubmed:affiliation | Department of Biology and Chemistry, City University of Hong Kong, 83 Tat Chee Avenue, Kowloon, Hong Kong, People's Republic of China. | lld:pubmed |
| pubmed-article:11772403 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11772403 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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