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Statements

Subject Item
n2:RIV%2F61388963%3A_____%2F11%3A00364221%21RIV12-AV0-61388963
rdf:type
skos:Concept n15:Vysledek
dcterms:description
We utilized a series of modified pyrimidine analogues to determine the mechanism used by human DNA polymerase α 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. We utilized a series of modified pyrimidine analogues to determine the mechanism used by human DNA polymerase α 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.
dcterms:title
B Family DNA Polymerases Asymmetrically Recognize Pyrimidines and Purines B Family DNA Polymerases Asymmetrically Recognize Pyrimidines and Purines
skos:prefLabel
B Family DNA Polymerases Asymmetrically Recognize Pyrimidines and Purines B Family DNA Polymerases Asymmetrically Recognize Pyrimidines and Purines
skos:notation
RIV/61388963:_____/11:00364221!RIV12-AV0-61388963
n15:predkladatel
n16:ico%3A61388963
n3:aktivita
n20:P n20:Z
n3:aktivity
P(IAA400550902), P(LC512), Z(AV0Z40550506)
n3:cisloPeriodika
33
n3:dodaniDat
n4:2012
n3:domaciTvurceVysledku
n8:6659160 Joubert, Nicolas
n3:druhVysledku
n14:J
n3:duvernostUdaju
n5:S
n3:entitaPredkladatele
n6:predkladatel
n3:idSjednocenehoVysledku
187728
n3:idVysledku
RIV/61388963:_____/11:00364221
n3:jazykVysledku
n12:eng
n3:klicovaSlova
active-site tightness; genetic alphabet; deoxynucleoside; phosphoramidites
n3:klicoveSlovo
n9:phosphoramidites n9:active-site%20tightness n9:genetic%20alphabet n9:deoxynucleoside
n3:kodStatuVydavatele
US - Spojené státy americké
n3:kontrolniKodProRIV
[F1F268603062]
n3:nazevZdroje
Biochemistry
n3:obor
n13:CC
n3:pocetDomacichTvurcuVysledku
2
n3:pocetTvurcuVysledku
7
n3:projekt
n10:LC512 n10:IAA400550902
n3:rokUplatneniVysledku
n4:2011
n3:svazekPeriodika
50
n3:tvurceVysledku
Lund, T. J. Kuchta, R. D. Urban, M. Cavanaugh, N. A. Patro, J. N. Hocek, Michal Joubert, Nicolas
n3:wos
000294076100018
n3:zamer
n19:AV0Z40550506
s:issn
0006-2960
s:numberOfPages
8
n17:doi
10.1021/bi2006916