Nucleotides with Altered Hydrogen Bonding Capacities Impede Human DNA Polymerase η by Reducing Synthesis in the Presence of the Major Cisplatin DNA Adduct

2015 ◽  
Vol 137 (14) ◽  
pp. 4728-4734 ◽  
Author(s):  
Arman Nilforoushan ◽  
Antonia Furrer ◽  
Laura A. Wyss ◽  
Barbara van Loon ◽  
Shana J. Sturla
Keyword(s):  
Hydrogen Bonding ◽  
Dna Polymerase ◽  
Dna Adduct ◽  
Human Dna

Human DNA polymerase λ catalyzes lesion bypass across benzo[a]pyrene-derived DNA adduct during base excision repair

DNA Repair ◽  
2012 ◽  
Vol 11 (4) ◽  
pp. 367-373 ◽  
Author(s):  
Lidia V. Skosareva ◽  
Natalia A. Lebedeva ◽  
Nadejda I. Rechkunova ◽  
Alexander Kolbanovskiy ◽  
Nicholas E. Geacintov ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Base Excision Repair ◽  
Excision Repair ◽  
Dna Adduct ◽  
Lesion Bypass ◽  
Human Dna ◽  
Dna Polymerase Λ ◽  
Base Excision

scholarly journals Translesion Synthesis past Acrolein-derived DNA Adduct, γ-Hydroxypropanodeoxyguanosine, by Yeast and Human DNA Polymerase η

2002 ◽  
Vol 278 (2) ◽  
pp. 784-790 ◽  
Author(s):  
Irina G. Minko ◽  
M. Todd Washington ◽  
Manorama Kanuri ◽  
Louise Prakash ◽  
Satya Prakash ◽  
...  
Keyword(s):  
Dna Polymerase ◽  
Translesion Synthesis ◽  
Dna Adduct ◽  
Human Dna

scholarly journals The abundant DNA adduct N7-methyl deoxyguanosine contributes to miscoding during replication by human DNA polymerase η

2019 ◽  
Vol 294 (26) ◽  
pp. 10253-10265 ◽  
Author(s):  
Olive J. Njuma ◽  
Yan Su ◽  
F. Peter Guengerich
Keyword(s):  
Dna Polymerase ◽  
Dna Adduct ◽  
Human Dna

scholarly journals Role of Hoogsteen Edge Hydrogen Bonding at Template Purines in Nucleotide Incorporation by Human DNA Polymerase ι

2006 ◽  
Vol 26 (17) ◽  
pp. 6435-6441 ◽  
Author(s):  
Robert E. Johnson ◽  
Lajos Haracska ◽  
Louise Prakash ◽  
Satya Prakash
Keyword(s):  
Hydrogen Bonding ◽  
Dna Polymerase ◽  
Active Site ◽  
Dna Polymerases ◽  
Human Dna ◽  
Nucleotide Incorporation ◽  
Template Specificity ◽  
Hydrogen Bonding Potential ◽  
Dna Polymerase Ι

ABSTRACT Human DNA polymerase ι (Pol ι) differs from other DNA polymerases in that it exhibits a marked template specificity, being more efficient and accurate opposite template purines than opposite pyrimidines. The crystal structures of Pol ι with template A and incoming dTTP and with template G and incoming dCTP have revealed that in the Pol ι active site, the templating purine adopts a syn conformation and forms a Hoogsteen base pair with the incoming pyrimidine which remains in the anti conformation. By using 2-aminopurine and purine as the templating residues, which retain the normal N7 position but lack the N6 of an A or the O6 of a G, here we provide evidence that whereas hydrogen bonding at N6 is dispensable for the proficient incorporation of a T opposite template A, hydrogen bonding at O6 is a prerequisite for C incorporation opposite template G. To further analyze the contributions of O6 and N7 hydrogen bonding to DNA synthesis by Pol ι, we have examined its proficiency for replicating through the 6 O-methyl guanine and 8-oxoguanine lesions, which affect the O6 and N7 positions of template G, respectively. We conclude from these studies that for proficient T incorporation opposite template A, only the N7 hydrogen bonding is required, but for proficient C incorporation opposite template G, hydrogen bonding at both the N7 and O6 is an imperative. The dispensability of N6 hydrogen bonding for proficient T incorporation opposite template A has important biological implications, as that would endow Pol ι with the ability to replicate through lesions which impair the Watson-Crick hydrogen bonding potential at both the N1 and N6 positions of templating A.

scholarly journals Lesion orientation of O4-alkylthymidine influences replication by human DNA polymerase η

2016 ◽  
Vol 7 (8) ◽  
pp. 4896-4904 ◽  
Author(s):  
D. K. O'Flaherty ◽  
A. Patra ◽  
Y. Su ◽  
F. P. Guengerich ◽  
M. Egli ◽  
...  
Keyword(s):  
Hydrogen Bonding ◽  
Crystal Structures ◽  
Dna Polymerase ◽  
Active Site ◽  
Ternary Complexes ◽  
Human Dna

Conformation of the α-carbon of O4-alkylthymidine was shown to exert an influence on human DNA polymerase η (hPol η) bypass. Crystal structures of hPol η·DNA·dNTP ternary complexes reveal a unique conformation adopted by O4-methylthymidine, where the nucleobase resides nestled at the active site ceiling where hydrogen-bonding with the incoming nucleotide is prevented.

Expression and Activity of Human DNA Polymerase ^|^eta; in Escherichia coli

2013 ◽  
Vol 35 (1) ◽  
pp. 10-20 ◽  
Author(s):  
Petr Gr^|^uacute;z ◽  
Takehiko Nohmi
Keyword(s):  
Escherichia Coli ◽  
Dna Polymerase ◽  
Polymerase Eta ◽  
Human Dna ◽  
Dna Polymerase Eta ◽  
Expression And Activity
Sign in / Sign up

Export Citation Format

Share Document