Autor: Urban, M.; Kuchta R. D.
Název práce v češtině: Mechanizmus, pomocí kterého DNA primázy volí , zda polymerizovat nukleosid trifosfát
Název práce v angličtině: Mechanisms by which DNA Primases Choose to Polymerize a Nucleoside Triphosphate

Klíčová slova v angličtině:DNA, RNA, primase, replication, primer

Abstrakt anglicky: DNA primases synthesize short RNA primers that other DNA polymerases then elongate during the DNA replication proces. Even though primases misincorporate NTPs at a relatively high frequency, this does not impact the final product DNA because the RNA primer is later replaced by DNA. We used an extensive series of purine and pyrimidine analogues to provide further insights into the mechanism by which primases choose wheather to polymerize a NTP or not. We studied herpes1 and human2 primase, two mechanistically related enzymes. We found that human primase strongly depends on Watson-Crick hydrogen bonds for efficient nucleotide polymerization; in contrast herpes primase sometimes tolerated base pairs that could not form a single hydrogen bond but in other cases removing single Watson-Crick bonding groups from either the NTP or templating bases completely blocked the polymerization. Both primases did not tolerate altered Watson-Crick hydrogen bonds in isoG-isoC base pair and most times did not incorporate NTP’s with hydrophobic bases.Additionally, we found that human and herpes primase can misincorporate nucleotide both by misreading the templare and by a primer – template slippage mechanism. Based on our data, we came with a model suggesting that the high error frequency of primase may result from primer – template instability rather than inherent inaccuracy; this model suggests biochemical rationale for the existence of primase.
Jazyk v originále: anglický
Publikace abstraktu: sbornik, 23/141
Forma prezentace: přednáška

Místo konání: Lázně Bělohrad (Czech Republic)