Two Essential DNA Polymerases at the Bacterial Replication Fork

Science ◽  
2001 ◽  
Vol 294 (5547) ◽  
pp. 1716-1719 ◽  
Author(s):  
E. Dervyn
Keyword(s):  
Replication Fork ◽  
Dna Polymerases ◽  
Bacterial Replication

Evidence from mutational specificity studies that yeast DNA polymerases δ and ϵ replicate different DNA strands at an intracellular replication fork 1 1Edited by A. R. Fersht

2000 ◽  
Vol 299 (2) ◽  
pp. 405-419 ◽  
Author(s):  
Ramachandran Karthikeyan ◽  
Edward J Vonarx ◽  
Andrew F.L Straffon ◽  
Michel Simon ◽  
Gérard Faye ◽  
...  
Keyword(s):  
Replication Fork ◽  
Dna Polymerases ◽  
Intracellular Replication ◽  
Mutational Specificity ◽  
Dna Strands

Uracil recognition by archaeal family B DNA polymerases

2003 ◽  
Vol 31 (3) ◽  
pp. 699-702 ◽  
Author(s):  
B.A. Connolly ◽  
M.J. Fogg ◽  
G. Shuttleworth ◽  
B.T. Wilson
Keyword(s):  
Dna Synthesis ◽  
Protein Interactions ◽  
Replication Fork ◽  
Dna Polymerases ◽  
Structural Basis ◽  
Dna Glycosylases ◽  
Protein Protein Interactions ◽  
Sensing Mechanism ◽  
Uridine Triphosphate

Archaeal family-B DNA polymerases possess a novel uracil-sensing mechanism. A specialized pocket scans the template, ahead of the replication fork, for the presence of uracil; on encountering this base, DNA synthesis is stalled. The structural basis for uracil recognition by polymerases is described and compared with other uracil-recognizing enzymes (uridine-triphosphate pyrophophatases and uracil-DNA glycosylases). Remarkably, protein–protein interactions between all three archaeal uracil sensors are observed; possibly the enzymes co-operate to efficiently eliminate uracil from archaeal genomes.

scholarly journals Two essential replicative DNA polymerases exchange dynamically during DNA replication and after replication fork arrest

2018 ◽  
Author(s):  
Yilai Li ◽  
Ziyuan Chen ◽  
Lindsay A. Matthews ◽  
Lyle A. Simmons ◽  
Julie S. Biteen
Keyword(s):  
Dna Replication ◽  
Single Molecule ◽  
Replication Fork ◽  
Dna Polymerases ◽  
Super Resolution ◽  
Clamp Loader ◽  
Chromosomal Dna ◽  
Chromosomal Replication ◽  
Replication Process ◽  
Cooperative Process

AbstractThe replisome is the multi-protein complex responsible for faithful replication of chromosomal DNA. Using single-molecule super-resolution imaging, we characterized the dynamics of three replisomal proteins in liveBacillus subtiliscells: the two replicative DNA polymerases, PolC and DnaE, and a processivity clamp loader subunit, DnaX. We quantified the protein mobility and dwell times during normal replication and following both damage-independent and damage-dependent replication fork stress. With these results, we report the dynamic and cooperative process of DNA replication based on changes in the measured diffusion coefficients and dwell times. These experiments show that the replisomal proteins are all highly dynamic and that the exchange rate depends on whether DNA synthesis is active or arrested. Our results also suggest coupling between PolC and DnaX in the DNA replication process, and indicate that DnaX provides an important role in synthesis during repair. Furthermore, our results show that DnaE provides a limited contribution to chromosomal replication and repair.

scholarly journals Translesion Synthesis Polymerases in the Prevention and Promotion of Carcinogenesis

2010 ◽  
Vol 2010 ◽  
pp. 1-10 ◽  
Author(s):  
L. Jay Stallons ◽  
W. Glenn McGregor
Keyword(s):  
Knockout Mouse ◽  
Replication Fork ◽  
Dna Polymerases ◽  
Altered Expression ◽  
Translesion Dna Synthesis ◽  
Environmental Agents ◽  
Malignant State ◽  
Copy Dna

A critical step in the transformation of cells to the malignant state of cancer is the induction of mutations in the DNA of cells damaged by genotoxic agents. Translesion DNA synthesis (TLS) is the process by which cells copy DNA containing unrepaired damage that blocks progression of the replication fork. The DNA polymerases that catalyze TLS in mammals have been the topic of intense investigation over the last decade. DNA polymeraseη(Polη) is best understood and is active in error-free bypass of UV-induced DNA damage. The other TLS polymerases (Pol ι, Pol κ, REV1, and Pol ζ) have been studied extensivelyin vitro, but theirin vivorole is only now being investigated using knockout mouse models of carcinogenesis. This paper will focus on the studies of mice and humans with altered expression of TLS polymerases and the effects on cancer induced by environmental agents.

scholarly journals DNA Polymerases at the Eukaryotic Replication Fork Thirty Years after: Connection to Cancer

Cancers ◽  
2020 ◽  
Vol 12 (12) ◽  
pp. 3489
Author(s):  
Youri I. Pavlov ◽  
Anna S. Zhuk ◽  
Elena I. Stepchenkova
Keyword(s):  
Replication Fork ◽  
Genome Instability ◽  
Dna Polymerases ◽  
Structure And Function ◽  
The Past ◽  
New Findings ◽  
Dna Strands ◽  
Leading Strand ◽  
And Function

Recent studies on tumor genomes revealed that mutations in genes of replicative DNA polymerases cause a predisposition for cancer by increasing genome instability. The past 10 years have uncovered exciting details about the structure and function of replicative DNA polymerases and the replication fork organization. The principal idea of participation of different polymerases in specific transactions at the fork proposed by Morrison and coauthors 30 years ago and later named “division of labor,” remains standing, with an amendment of the broader role of polymerase δ in the replication of both the lagging and leading DNA strands. However, cancer-associated mutations predominantly affect the catalytic subunit of polymerase ε that participates in leading strand DNA synthesis. We analyze how new findings in the DNA replication field help elucidate the polymerase variants’ effects on cancer.

scholarly journals Correction: Pavlov, Y.I., et al. DNA Polymerases at the Eukaryotic Replication Fork Thirty Years After: Connection to Cancer. Cancers 2020, 12, 3489

Cancers ◽  
2021 ◽  
Vol 13 (5) ◽  
pp. 969
Author(s):  
Youri I. Pavlov ◽  
Anna S. Zhuk ◽  
Elena I. Stepchenkova
Keyword(s):  
Replication Fork ◽  
Dna Polymerases

The authors wish to make the following corrections to this paper [...]

scholarly journals Plant organellar DNA polymerases bypass thymine glycol using two conserved lysine residues

2020 ◽  
Vol 477 (5) ◽  
pp. 1049-1059 ◽  
Author(s):  
Noe Baruch-Torres ◽  
Junpei Yamamoto ◽  
Víctor Juárez-Quintero ◽  
Shigenori Iwai ◽  
Luis G. Brieba
Keyword(s):  
Structural Model ◽  
Dna Polymerases ◽  
Lesion Bypass ◽  
Thymine Glycol ◽  
Abasic Sites ◽  
Organellar Dna ◽  
Lysine Residues ◽  
Exogenous Agents ◽  
Replicative Polymerases ◽  
Bacterial Replication

Plant organelles cope with endogenous DNA damaging agents, byproducts of respiration and photosynthesis, and exogenous agents like ultraviolet light. Plant organellar DNA polymerases (DNAPs) are not phylogenetically related to yeast and metazoan DNAPs and they harbor three insertions not present in any other DNAPs. Plant organellar DNAPs from Arabidopsis thaliana (AtPolIA and AtPolIB) are translesion synthesis (TLS) DNAPs able to bypass abasic sites, a lesion that poses a strong block to replicative polymerases. Besides abasic sites, reactive oxidative species and ionizing radiation react with thymine resulting in thymine glycol (Tg), a DNA adduct that is also a strong block to replication. Here, we report that AtPolIA and AtPolIB bypass Tg by inserting an adenine opposite the lesion and efficiently extend from a Tg-A base pair. The TLS ability of AtPolIB is mapped to two conserved lysine residues: K593 and K866. Residue K593 is situated in insertion 1 and K866 is in insertion 3. With basis on the location of both insertions on a structural model of AtPolIIB, we hypothesize that the two positively charged residues interact to form a clamp around the primer-template. In contrast with nuclear and bacterial replication, where lesion bypass involves an interplay between TLS and replicative DNA polymerases, we postulate that plant organellar DNAPs evolved to exert replicative and TLS activities.

Sign in / Sign up

Export Citation Format

Share Document