Characterization of Mycobacterium smegmatis PolD2 and PolD1 as RNA/DNA Polymerases Homologous to the POL Domain of Bacterial DNA Ligase D
Author:
Affiliation:
1. Molecular Biology Program and ‡Immunology Program, Sloan-Kettering Institute, New York, New York 10065, United States
Publisher
American Chemical Society (ACS)
Subject
Biochemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/bi301202e
Reference30 articles.
1. The Mechanism of Double-Strand DNA Break Repair by the Nonhomologous DNA End-Joining Pathway
2. Bacterial DNA repair by non-homologous end joining
3. A Primer-dependent Polymerase Function of Pseudomonas aeruginosa ATP-dependent DNA Ligase (LigD)
4. Atomic structure and nonhomologous end-joining function of the polymerase component of bacterial DNA ligase D
5. Nucleotide Misincorporation, 3′-Mismatch Extension, and Responses to Abasic Sites and DNA Adducts by the Polymerase Component of Bacterial DNA Ligase D
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