Mutant forms of theEscherichia coliβ sliding clamp that distinguish between its roles in replication and DNA polymerase V-dependent translesion DNA synthesis

2005 ◽  
Vol 55 (6) ◽  
pp. 1751-1766 ◽  
Author(s):  
Mark D. Sutton ◽  
Jill M. Duzen ◽  
Robert W. Maul
Keyword(s):  
Dna Synthesis ◽  
Dna Polymerase ◽  
Translesion Dna Synthesis ◽  
Sliding Clamp ◽  
Dna Polymerase V ◽  
Translesion Dna ◽  
Mutant Forms

scholarly journals Investigating the role of the E. coli β‐sliding clamp in DNA polymerase V‐dependent translesion DNA synthesis

2006 ◽  
Vol 20 (5) ◽  
Author(s):  
Mark David Sutton ◽  
Laurie Sanders ◽  
Sarah Ponticelli ◽  
Jill Duzen ◽  
Robert Maul ◽  
...  
Keyword(s):  
Dna Synthesis ◽  
Dna Polymerase ◽  
Translesion Dna Synthesis ◽  
E Coli ◽  
Sliding Clamp ◽  
Dna Polymerase V ◽  
Translesion Dna

scholarly journals The SOS Error-Prone DNA Polymerase V Mutasome and β-Sliding Clamp Acting in Concert on Undamaged DNA and during Translesion Synthesis

Cells ◽  
2021 ◽  
Vol 10 (5) ◽  
pp. 1083
Author(s):  
Adhirath Sikand ◽  
Malgorzata Jaszczur ◽  
Linda B. Bloom ◽  
Roger Woodgate ◽  
Michael M. Cox ◽  
...  
Keyword(s):  
Dna Synthesis ◽  
Dna Polymerase ◽  
Pathogenic Bacteria ◽  
Fold Increase ◽  
Translesion Dna Synthesis ◽  
Sliding Clamp ◽  
Pol V ◽  
Dna Polymerase V ◽  
Acting In Concert

In the mid 1970s, Miroslav Radman and Evelyn Witkin proposed that Escherichia coli must encode a specialized error-prone DNA polymerase (pol) to account for the 100-fold increase in mutations accompanying induction of the SOS regulon. By the late 1980s, genetic studies showed that SOS mutagenesis required the presence of two “UV mutagenesis” genes, umuC and umuD, along with recA. Guided by the genetics, decades of biochemical studies have defined the predicted error-prone DNA polymerase as an activated complex of these three gene products, assembled as a mutasome, pol V Mut = UmuD’2C-RecA-ATP. Here, we explore the role of the β-sliding processivity clamp on the efficiency of pol V Mut-catalyzed DNA synthesis on undamaged DNA and during translesion DNA synthesis (TLS). Primer elongation efficiencies and TLS were strongly enhanced in the presence of β. The results suggest that β may have two stabilizing roles: its canonical role in tethering the pol at a primer-3’-terminus, and a possible second role in inhibiting pol V Mut’s ATPase to reduce the rate of mutasome-DNA dissociation. The identification of umuC, umuD, and recA homologs in numerous strains of pathogenic bacteria and plasmids will ensure the long and productive continuation of the genetic and biochemical journey initiated by Radman and Witkin.

Protein interactions in T7 DNA replisome inhibit the bypass of abasic site by DNA polymerase

Mutagenesis ◽  
2019 ◽  
Author(s):  
Zhenyu Zou ◽  
Tingting Liang ◽  
Zhongyan Xu ◽  
Jiayu Xie ◽  
Shuming Zhang ◽  
...  
Keyword(s):  
Dna Replication ◽  
Dna Synthesis ◽  
Dna Polymerase ◽  
Protein Interactions ◽  
Accessory Proteins ◽  
Abasic Site ◽  
Traditional Concept ◽  
Translesion Dna Synthesis ◽  
Dna Lesion ◽  
Translesion Dna

Abstract Abasic site as a common DNA lesion blocks DNA replication and is highly mutagenic. Protein interactions in T7 DNA replisome facilitate DNA replication and translesion DNA synthesis. However, bypass of an abasic site by T7 DNA replisome has never been investigated. In this work, we used T7 DNA replisome and T7 DNA polymerase alone as two models to study DNA replication on encountering an abasic site. Relative to unmodified DNA, abasic site strongly inhibited primer extension and completely blocked strand-displacement DNA synthesis, due to the decreased fraction of enzyme–DNA productive complex and the reduced average extension rates. Moreover, abasic site at DNA fork inhibited the binding of DNA polymerase or helicase onto fork and the binding between polymerase and helicase at fork. Notably and unexpectedly, we found DNA polymerase alone bypassed an abasic site on primer/template (P/T) substrate more efficiently than did polymerase and helicase complex bypass it at fork. The presence of gp2.5 further inhibited the abasic site bypass at DNA fork. Kinetic analysis showed that this inhibition at fork relative to that on P/T was due to the decreased fraction of productive complex instead of the average extension rates. Therefore, we found that protein interactions in T7 DNA replisome inhibited the bypass of DNA lesion, different from all the traditional concept that protein interactions or accessory proteins always promote DNA replication and DNA damage bypass, providing new insights in translesion DNA synthesis performed by DNA replisome.

scholarly journals Mechanism of Translesion DNA Synthesis by DNA Polymerase II

1996 ◽  
Vol 271 (40) ◽  
pp. 24662-24669 ◽  
Author(s):  
Tamar Paz-Elizur ◽  
Masaru Takeshita ◽  
Myron Goodman ◽  
Michael O'Donnell ◽  
Zvi Livneh
Keyword(s):  
Dna Synthesis ◽  
Dna Polymerase ◽  
Translesion Dna Synthesis ◽  
Translesion Dna ◽  
Dna Polymerase Ii

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.

Sign in / Sign up

Export Citation Format

Share Document