B Family DNA Polymerases Asymmetrically Recognize Pyrimidines and Purines
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F11%3A00364221" target="_blank" >RIV/61388963:_____/11:00364221 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1021/bi2006916" target="_blank" >http://dx.doi.org/10.1021/bi2006916</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1021/bi2006916" target="_blank" >10.1021/bi2006916</a>
Alternative languages
Result language
angličtina
Original language name
B Family DNA Polymerases Asymmetrically Recognize Pyrimidines and Purines
Original language description
We utilized a series of modified pyrimidine analogues to determine the mechanism used by human DNA polymerase ? and herpes simplex virus I DNA polymerase to polymerize pyrimidine dNTPs. Removing O2 of a pyrimidine dNTP vastly decreased incorporation by these enzymes and also compromised fidelity in the case of C analogues, while removing O2 from the templating base had more modest effects. Removing the Watson-Crick hydrogen bonding groups greatly impaired polymerization. The Watson-Crick hydrogen bonding plays an important role in enhancing correct dNTP polymerization, but are not essential for preventing misincorporation. These studies also indicate that DNA polymerases recognize bases extremely asymmetrically, both in terms of whether they are a purine or pyrimidine and whether they are in the template or are the incoming dNTP. The mechanistic implications of these results regarding how polymerases discriminate between right and wrong dNTPs are discussed.
Czech name
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Czech description
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Classification
Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
CC - Organic chemistry
OECD FORD branch
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Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)
Others
Publication year
2011
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Biochemistry
ISSN
0006-2960
e-ISSN
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Volume of the periodical
50
Issue of the periodical within the volume
33
Country of publishing house
US - UNITED STATES
Number of pages
8
Pages from-to
7243-7250
UT code for WoS article
000294076100018
EID of the result in the Scopus database
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