Human DNA Polymerases λ and β Show Different Efficiencies of Translesion DNA Synthesis past Abasic Sites and Alternative Mechanisms for Frameshift Generation†

Biochemistry ◽  
2004 ◽  
Vol 43 (36) ◽  
pp. 11605-11615 ◽  
Author(s):  
Giuseppina Blanca ◽  
Giuseppe Villani ◽  
Igor Shevelev ◽  
Kristijan Ramadan ◽  
Silvio Spadari ◽  
...  
Keyword(s):  
Dna Synthesis ◽  
Dna Polymerases ◽  
Translesion Dna Synthesis ◽  
Abasic Sites ◽  
Human Dna ◽  
Translesion Dna

scholarly journals In VitroGap-directed Translesion DNA Synthesis of an Abasic Site Involving Human DNA Polymerases ϵ, λ, and β

2011 ◽  
Vol 286 (37) ◽  
pp. 32094-32104 ◽  
Author(s):  
Giuseppe Villani ◽  
Ulrich Hubscher ◽  
Nadege Gironis ◽  
Sinikka Parkkinen ◽  
Helmut Pospiech ◽  
...  
Keyword(s):  
Dna Synthesis ◽  
Dna Polymerases ◽  
Abasic Site ◽  
Translesion Dna Synthesis ◽  
Human Dna ◽  
Translesion Dna

scholarly journals Trading Places: How Do DNA Polymerases Switch during Translesion DNA Synthesis?

2005 ◽  
Vol 19 (1) ◽  
pp. 143
Author(s):  
Errol C. Friedberg ◽  
Alan R. Lehmann ◽  
Robert P.P. Fuchs
Keyword(s):  
Dna Synthesis ◽  
Dna Polymerases ◽  
Translesion Dna Synthesis ◽  
Translesion Dna

Translesion DNA synthesis across double-base lesions derived from cross-links of an antitumor trinuclear platinum compound: primer extension, conformational and thermodynamic studies

Metallomics ◽  
2018 ◽  
Vol 10 (1) ◽  
pp. 132-144 ◽  
Author(s):  
O. Novakova ◽  
N. P. Farrell ◽  
V. Brabec
Keyword(s):  
Dna Synthesis ◽  
Dna Polymerases ◽  
Primer Extension ◽  
Platinum Compound ◽  
Thermodynamic Studies ◽  
Translesion Dna Synthesis ◽  
Cross Links ◽  
Translesion Dna ◽  
Compound Primer ◽  
Double Base

The central linker of antitumor polynuclear Triplatin represents an important factor responsible for the lowered tolerance of its DNA double-base adducts by DNA polymerases.

scholarly journals N-terminal domains of human DNA polymerase lambda promote primer realignment during translesion DNA synthesis

DNA Repair ◽  
2014 ◽  
Vol 22 ◽  
pp. 41-52 ◽  
Author(s):  
David J. Taggart ◽  
Daniel M. Dayeh ◽  
Saul W. Fredrickson ◽  
Zucai Suo
Keyword(s):  
Dna Synthesis ◽  
Dna Polymerase ◽  
Translesion Dna Synthesis ◽  
Human Dna ◽  
Translesion Dna ◽  
Terminal Domains

scholarly journals Transcriptional Modulator NusA Interacts with Translesion DNA Polymerases in Escherichia coli

2008 ◽  
Vol 191 (2) ◽  
pp. 665-672 ◽  
Author(s):  
Susan E. Cohen ◽  
Veronica G. Godoy ◽  
Graham C. Walker
Keyword(s):  
Escherichia Coli ◽  
Rna Polymerase ◽  
Dna Synthesis ◽  
Dna Polymerase ◽  
Temperature Sensitivity ◽  
Dna Polymerases ◽  
Rna Polymerases ◽  
Translesion Dna Synthesis ◽  
Catalytic Activities ◽  
Translesion Dna

ABSTRACT NusA, a modulator of RNA polymerase, interacts with the DNA polymerase DinB. An increased level of expression of dinB or umuDC suppresses the temperature sensitivity of the nusA11 strain, requiring the catalytic activities of these proteins. We propose that NusA recruits translesion DNA synthesis (TLS) polymerases to RNA polymerases stalled at gaps, coupling TLS to transcription.

scholarly journals Enzymatic Switching Between Archaeal DNA Polymerases Facilitates Abasic Site Bypass

2021 ◽  
Vol 12 ◽  
Author(s):  
Xu Feng ◽  
Baochang Zhang ◽  
Ruyi Xu ◽  
Zhe Gao ◽  
Xiaotong Liu ◽  
...  
Keyword(s):  
Dna Synthesis ◽  
Enzyme Kinetics ◽  
Dna Polymerases ◽  
Dna Lesions ◽  
Abasic Site ◽  
Lesion Bypass ◽  
Translesion Dna Synthesis ◽  
Kinetics Studies ◽  
Abasic Sites ◽  
Y Family

Abasic sites are among the most abundant DNA lesions encountered by cells. Their replication requires actions of specialized DNA polymerases. Herein, two archaeal specialized DNA polymerases were examined for their capability to perform translesion DNA synthesis (TLS) on the lesion, including Sulfolobuss islandicus Dpo2 of B-family, and Dpo4 of Y-family. We found neither Dpo2 nor Dpo4 is efficient to complete abasic sites bypass alone, but their sequential actions promote lesion bypass. Enzyme kinetics studies further revealed that the Dpo4’s activity is significantly inhibited at +1 to +3 site past the lesion, at which Dpo2 efficiently extends the primer termini. Furthermore, their activities are inhibited upon synthesis of 5–6 nt TLS patches. Once handed over to Dpo1, these substrates basically inactivate its exonuclease, enabling the transition from proofreading to polymerization of the replicase. Collectively, by functioning as an “extender” to catalyze further DNA synthesis past the lesion, Dpo2 bridges the activity gap between Dpo4 and Dpo1 in the archaeal TLS process, thus achieving more efficient lesion bypass.

scholarly journals When DNA Polymerases Multitask: Functions Beyond Nucleotidyl Transfer

2022 ◽  
Vol 8 ◽  
Author(s):  
Denisse Carvajal-Maldonado ◽  
Lea Drogalis Beckham ◽  
Richard D. Wood ◽  
Sylvie Doublié
Keyword(s):  
Dna Repair ◽  
Dna Replication ◽  
Dna Synthesis ◽  
Extracurricular Activities ◽  
Damage Tolerance ◽  
Dna Polymerases ◽  
Translesion Dna Synthesis ◽  
Dna Strands ◽  
Translesion Dna ◽  
Central Reaction

DNA polymerases catalyze nucleotidyl transfer, the central reaction in synthesis of DNA polynucleotide chains. They function not only in DNA replication, but also in diverse aspects of DNA repair and recombination. Some DNA polymerases can perform translesion DNA synthesis, facilitating damage tolerance and leading to mutagenesis. In addition to these functions, many DNA polymerases conduct biochemically distinct reactions. This review presents examples of DNA polymerases that carry out nuclease (3ʹ—5′ exonuclease, 5′ nuclease, or end-trimming nuclease) or lyase (5′ dRP lyase) extracurricular activities. The discussion underscores how DNA polymerases have a remarkable ability to manipulate DNA strands, sometimes involving relatively large intramolecular movement.

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