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Creative template-dependent synthesis by human polymerase mu.

Andrea F Moon1, Rajendrakumar A Gosavi1, Thomas A Kunkel1

  • 1Genome Integrity and Structural Biology Laboratory, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC 27709.

Proceedings of the National Academy of Sciences of the United States of America
|August 5, 2015
PubMed
Summary
This summary is machine-generated.

DNA polymerase mu (Pol µ) exhibits unique gap-filling behavior during DNA repair. Unlike Pol lambda, Pol µ skips the first nucleotide, using the template base at the gap

Keywords:
DNA polymerase lambdaDNA polymerase muDNA repairnonhomologous end joining

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Nonhomologous end joining (NHEJ) is a crucial DNA repair pathway.
  • Family X DNA polymerases, including Pol λ and Pol µ, are involved in NHEJ.
  • Polymerase choice depends on DNA break sequence complementarity.

Purpose of the Study:

  • To elucidate the substrate preferences of Pol µ during NHEJ.
  • To understand the structural basis for Pol µ's distinct gap-filling mechanism.

Main Methods:

  • X-ray crystallography of Pol µ bound to a gapped DNA substrate.
  • Analysis of three catalytic cycle steps.

Main Results:

  • Pol µ displays a novel gap-filling mechanism, distinct from Pol λ.
  • Pol µ skips the initial template nucleotide within the gap.
  • It utilizes the template base at the 5' end of the gap for nucleotide incorporation.

Conclusions:

  • Pol µ's unique mechanism explains its substrate specificity in NHEJ.
  • This finding provides insights into polymerase selection during DNA repair.
  • The study reveals a divergence from canonical 3'-end gap filling strategies.