Human DNA ligase IV and the ligase IV/XRCC4 complex: analysis of nick ligation fidelity.

Human DNA ligase IV and the ligase IV/XRCC4 complex: analysis of nick ligation fidelity. Research Abstract Details 

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Human DNA ligase IV and the ligase IV/XRCC4 complex: analysis of nick ligation fidelity. Abstract Text:

Yu Wang,Brandon J Lamarche,Ming-Daw Tsai,

In addition to linking nicked/fragmented DNA molecules back into a contiguous duplex, DNA ligases also have the capacity to influence the accuracy of DNA repair pathways via their tolerance/intolerance of nicks containing mismatched base pairs. Although human DNA ligase I (Okazaki fragment processing) and the human DNA ligase III/XRCC1 complex (general DNA repair) have been shown to be relatively intolerant of nicks containing mismatched base pairs, the human DNA ligase IV/XRCC4 complex has not been studied in this regard. Ligase IV/XRCC4 is the sole DNA ligase involved in the repair of double strand breaks (DSBs) via the non-homologous end joining (NHEJ) pathway. During the repair of DSBs generated by chemical/physical damage as well as the repair of the programmed DSB intermediates of V(D)J recombination, there are scenarios where, at least conceptually, a capacity for ligating nicks containing mismatched base pairs would appear to be advantageous. Herein we examine whether ligase IV/XRCC4 can contribute a mismatched nick ligation activity to NHEJ. Toward this end, we (i) describe an E. coli-based coexpression system that provides relatively high yields of the ligase IV/XRCC4 complex, (ii) describe a unique rate-limiting step, which has bearing on how the complex is assayed, (iii) specifically analyze how XRCC4 influences ligase IV catalysis and substrate specificity, and (iv) probe the mismatch tolerance/intolerance of DNA ligase IV/XRCC4 via quantitative in vitro kinetic analyses. Analogous to most other DNA ligases, ligase IV/XRCC4 is shown to be fairly intolerant of nicks containing mismatched base pairs. These results are discussed in light of the biological roles of NHEJ.

Human DNA ligase IV and the ligase IV/XRCC4 complex: analysis of nick ligation fidelity. Publishing Authors By Initials

Y Wang,BJ Lamarche,MD Tsai,

For similar animals: chordata: vertebrates: mammals: primates: haplorhini: catarrhini: hominidae: humans research abstracts see: animals: chordata: vertebrates: mammals: primates: haplorhini: catarrhini: hominidae: humans research

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MEDLINE DATE:

Human DNA ligase IV and the ligase IV/XRCC4 complex: analysis of nick ligation fidelity. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: Biochemistry

VOLUME: 46

Page Numbers: 4962-76

Journal Abbreviation:

ISSN: 0006-2960

DAY: 4

MONTH: 04

YEAR: 2007

Human DNA ligase IV and the ligase IV/XRCC4 complex: analysis of nick ligation fidelity. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 370623

Human DNA ligase IV and the ligase IV/XRCC4 complex: analysis of nick ligation fidelity. Keywords Mesh Terms:

KEYWORDS: Humans

MESH TERMS: chemistry

Chemical & Substance for Abstract: Human DNA ligase IV and the ligase IV/XRCC4 complex: analysis of nick ligation fidelity. Information

Substance Name: DNA ligase (ATP)

Registry Number: EC 6.5.1.1

Grant and Affiliation Information for Human DNA ligase IV and the ligase IV/XRCC4 complex: analysis of nick ligation fidelity.

AFFILIATION: Department of Chemistry, The Ohio State University, Columbus, Ohio 43210, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: GM43268

ACRONYM: GM

MEDLINETA: Biochemistry

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