Literature DB >> 33087269

DNA polymerase mu: An inflexible scaffold for substrate flexibility.

Andrea M Kaminski1, Katarzyna Bebenek1, Lars C Pedersen1, Thomas A Kunkel2.   

Abstract

DNA polymerase μ is a Family X member that participates in repair of DNA double strand breaks (DSBs) by non-homologous end joining. Its role is to fill short gaps arising as intermediates in the process of V(D)J recombination and during processing of accidental double strand breaks. Pol μ is the only known template-dependent polymerase that can repair non-complementary DSBs with unpaired 3´primer termini. Here we review the unique properties of Pol μ that allow it to productively engage such a highly unstable substrate to generate a nick that can be sealed by DNA Ligase IV.
Copyright © 2020. Published by Elsevier B.V.

Entities:  

Keywords:  DNA double strand break repair; DNA polymerase μ; Family X DNA polymerases; Nonhomologous end-joining

Mesh:

Substances:

Year:  2020        PMID: 33087269      PMCID: PMC8713560          DOI: 10.1016/j.dnarep.2020.102932

Source DB:  PubMed          Journal:  DNA Repair (Amst)        ISSN: 1568-7856


  25 in total

1.  Creative template-dependent synthesis by human polymerase mu.

Authors:  Andrea F Moon; Rajendrakumar A Gosavi; Thomas A Kunkel; Lars C Pedersen; Katarzyna Bebenek
Journal:  Proc Natl Acad Sci U S A       Date:  2015-08-03       Impact factor: 11.205

2.  Molecular insights into DNA polymerase deterrents for ribonucleotide insertion.

Authors:  Nisha A Cavanaugh; William A Beard; Vinod K Batra; Lalith Perera; Lee G Pedersen; Samuel H Wilson
Journal:  J Biol Chem       Date:  2011-07-06       Impact factor: 5.157

Review 3.  Nonhomologous end joining: a good solution for bad ends.

Authors:  Crystal A Waters; Natasha T Strande; David W Wyatt; John M Pryor; Dale A Ramsden
Journal:  DNA Repair (Amst)       Date:  2014-03-14

4.  Sustained active site rigidity during synthesis by human DNA polymerase μ.

Authors:  Andrea F Moon; John M Pryor; Dale A Ramsden; Thomas A Kunkel; Katarzyna Bebenek; Lars C Pedersen
Journal:  Nat Struct Mol Biol       Date:  2014-02-02       Impact factor: 15.369

5.  Unexpected behavior of DNA polymerase Mu opposite template 8-oxo-7,8-dihydro-2'-guanosine.

Authors:  Andrea M Kaminski; Kishore K Chiruvella; Dale A Ramsden; Thomas A Kunkel; Katarzyna Bebenek; Lars C Pedersen
Journal:  Nucleic Acids Res       Date:  2019-09-26       Impact factor: 16.971

6.  Binary complex crystal structure of DNA polymerase β reveals multiple conformations of the templating 8-oxoguanine lesion.

Authors:  Vinod K Batra; David D Shock; William A Beard; Charles E McKenna; Samuel H Wilson
Journal:  Proc Natl Acad Sci U S A       Date:  2011-12-16       Impact factor: 11.205

7.  Polymerase mu is a DNA-directed DNA/RNA polymerase.

Authors:  Stephanie A Nick McElhinny; Dale A Ramsden
Journal:  Mol Cell Biol       Date:  2003-04       Impact factor: 4.272

8.  Role of the catalytic metal during polymerization by DNA polymerase lambda.

Authors:  Miguel Garcia-Diaz; Katarzyna Bebenek; Joseph M Krahn; Lars C Pedersen; Thomas A Kunkel
Journal:  DNA Repair (Amst)       Date:  2007-05-01

9.  Structural accommodation of ribonucleotide incorporation by the DNA repair enzyme polymerase Mu.

Authors:  Andrea F Moon; John M Pryor; Dale A Ramsden; Thomas A Kunkel; Katarzyna Bebenek; Lars C Pedersen
Journal:  Nucleic Acids Res       Date:  2017-09-06       Impact factor: 16.971

10.  A strategically located serine residue is critical for the mutator activity of DNA polymerase IV from Escherichia coli.

Authors:  Amit Sharma; Jithesh Kottur; Naveen Narayanan; Deepak T Nair
Journal:  Nucleic Acids Res       Date:  2013-03-21       Impact factor: 16.971

View more
  1 in total

Review 1.  Structural insights into the role of DNA-PK as a master regulator in NHEJ.

Authors:  Siyu Chen; James P Lees-Miller; Yuan He; Susan P Lees-Miller
Journal:  Genome Instab Dis       Date:  2021-07-23
  1 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.