Special Issue "DNA Polymerases: From the Maintenance of Genetic Information to Applications in Biotechnology and Biomedicine"

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Biochemistry".

Deadline for manuscript submissions: 1 May 2020.

Special Issue Editor

Dr. Modesto Redrejo Rodriguez
E-Mail Website
Guest Editor
Biochemistry Department and Instituto de Investigaciones Biológicas Alberto Sols, Universidad Autónoma de Madrid, Madrid, Spain
Interests: DNA replication, DNA repair, DNA polymerases, DNA amplification, DNA priming, protein engineering, translesion synthesis, genotoxic agents, DNA virus, transposon

Special Issue Information

Dear Colleagues,

Many applications with fundamental importance in modern molecular biology and biomedicine, including polymerase chain reaction (PCR) and whole genome DNA amplification (WGA), as well as some of the state-of-the-art DNA sequencing technologies, would not be feasible without the advances made in characterizing the DNA polymerases (DNAPs) during the last 60 years. Furthermore, the development of WGA at the single-cell and single-molecule level has contributed to some of the most recent breakthroughs in our knowledge of different complex biological systems—from microbial ecosystems, shedding light into microbial dark matter, to human disease, enhancing the sensitivity to detect genetic variants and mutation profiles of individual cells in a tissue or tumor, as well as changing the paradigms in the early diagnosis of cancer and genetic diseases with non-invasive genetic tests. Furthermore, beyond biotechnology applications, DNAPs are the enzymes responsible for preserving genetic information by replicating and repairing nucleic acid molecules in the cells. In the last years, novel developments and experimental approaches have led to a reevaluation of several accepted mechanisms, and have changed many paradigms in the DNA replication and repair field. This Special Issue will cover new advances on the structure, function, and biological role of DNA polymerases, both well-characterized and new, previously overlooked members with unexpected features, including AEPs, like bacterial LigD or PrimPols.

Dr. Modesto Redrejo Rodriguez
Guest Editor

Manuscript Submission Information

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Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Biomolecules is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1200 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • DNA polymerase
  • DNA replication
  • DNA repair
  • TLS
  • DNA amplification
  • MDA
  • PCR
  • biotechnology

Published Papers (1 paper)

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Research

Open AccessArticle
The Loop of the TPR1 Subdomain of Phi29 DNA Polymerase Plays a Pivotal Role in Primer-Terminus Stabilization at the Polymerization Active Site
Biomolecules 2019, 9(11), 648; https://doi.org/10.3390/biom9110648 - 24 Oct 2019
Abstract
Bacteriophage Phi29 DNA polymerase belongs to the protein-primed subgroup of family B DNA polymerases that use a terminal protein (TP) as a primer to initiate genome replication. The resolution of the crystallographic structure showed that it consists of an N-terminal domain with the [...] Read more.
Bacteriophage Phi29 DNA polymerase belongs to the protein-primed subgroup of family B DNA polymerases that use a terminal protein (TP) as a primer to initiate genome replication. The resolution of the crystallographic structure showed that it consists of an N-terminal domain with the exonuclease activity and a C-terminal polymerization domain. It also has two subdomains specific of the protein-primed DNA polymerases; the TP Regions 1 (TPR1) that interacts with TP and DNA, and 2 (TPR2), that couples both processivity and strand displacement to the enzyme. The superimposition of the structures of the apo polymerase and the polymerase in the polymerase/TP heterodimer shows that the structural changes are restricted almost to the TPR1 loop (residues 304–314). In order to study the role of this loop in binding the DNA and the TP, we changed the residues Arg306, Arg308, Phe309, Tyr310, and Lys311 into alanine, and also made the deletion mutant Δ6 lacking residues Arg306–Lys311. The results show a defective TP binding capacity in mutants R306A, F309A, Y310A, and Δ6. The additional impaired primer-terminus stabilization at the polymerization active site in mutants Y310A and Δ6 allows us to propose a role for the Phi29 DNA polymerase TPR1 loop in the proper positioning of the DNA and TP-priming 3’-OH termini at the preinsertion site of the polymerase to enable efficient initiation and further elongation steps during Phi29 TP-DNA replication. Full article
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