scholarly journals Human DNA Ligase IV and the Ligase IV/XRCC4 Complex:  Analysis of Nick Ligation Fidelity†

Biochemistry ◽  
2007 ◽  
Vol 46 (17) ◽  
pp. 4962-4976 ◽  
Author(s):  
Yu Wang ◽  
Brandon J. Lamarche ◽  
Ming-Daw Tsai
Keyword(s):  
Complex Analysis ◽  
Dna Ligase ◽  
Dna Ligase Iv ◽  
Human Dna ◽  
Ligase Iv

scholarly journals A High-Throughput Scintillation Proximity-Based Assay for Human DNA Ligase IV

2012 ◽  
Vol 10 (3) ◽  
pp. 235-249 ◽  
Author(s):  
Hui-Min Tseng ◽  
David Shum ◽  
Bhavneet Bhinder ◽  
Sindy Escobar ◽  
Nicholas J. Veomett ◽  
...  
Keyword(s):  
High Throughput ◽  
Dna Ligase ◽  
Dna Ligase Iv ◽  
Human Dna ◽  
Ligase Iv

scholarly journals In Vitro and In Vivo Interactions of DNA Ligase IV with a Subunit of the Condensin Complex

2003 ◽  
Vol 14 (2) ◽  
pp. 685-697 ◽  
Author(s):  
Marcin R. Przewloka ◽  
Paige E. Pardington ◽  
Steven M. Yannone ◽  
David J. Chen ◽  
Robert B. Cary
Keyword(s):  
Molecular Mechanisms ◽  
Critical Role ◽  
Dna Ligase ◽  
Mitotic Chromosomes ◽  
Dna Ligase Iv ◽  
Cell Extracts ◽  
Condensin Complex ◽  
Human Dna ◽  
Ligase Iv

Several findings have revealed a likely role for DNA ligase IV, and interacting protein XRCC4, in the final steps of mammalian DNA double-strand break repair. Recent evidence suggests that the human DNA ligase IV protein plays a critical role in the maintenance of genomic stability. To identify protein–protein interactions that may shed further light on the molecular mechanisms of DSB repair and the biological roles of human DNA ligase IV, we have used the yeast two-hybrid system in conjunction with traditional biochemical methods. These efforts have resulted in the identification of a physical association between the DNA ligase IV polypeptide and the human condensin subunit known as hCAP-E. The hCAP-E polypeptide, a member of the Structural Maintenance of Chromosomes (SMC) super-family of proteins, coimmunoprecipitates from cell extracts with DNA ligase IV. Immunofluorescence studies reveal colocalization of DNA ligase IV and hCAP-E in the interphase nucleus, whereas mitotic cells display colocalization of both polypeptides on mitotic chromosomes. Strikingly, the XRCC4 protein is excluded from the area of mitotic chromosomes, suggesting the formation of specialized DNA ligase IV complexes subject to cell cycle regulation. We discuss our findings in light of known and hypothesized roles for ligase IV and the condensin complex.

scholarly journals Structural Insights into the Role of Domain Flexibility in Human DNA Ligase IV

Structure ◽  
2012 ◽  
Vol 20 (7) ◽  
pp. 1212-1222 ◽  
Author(s):  
Takashi Ochi ◽  
Qian Wu ◽  
Dimitri Y. Chirgadze ◽  
J. Günter Grossmann ◽  
Victor M. Bolanos-Garcia ◽  
...  
Keyword(s):  
Dna Ligase ◽  
Dna Ligase Iv ◽  
Human Dna ◽  
Ligase Iv ◽  
Structural Insights

scholarly journals NAD+ is not utilized as a co-factor for DNA ligation by human DNA ligase IV

2020 ◽  
Vol 48 (22) ◽  
pp. 12746-12750
Author(s):  
Bailin Zhao ◽  
Tasmin Naila ◽  
Michael R Lieber ◽  
Alan E Tomkinson
Keyword(s):  
Strand Break ◽  
Dna Ligase ◽  
Unexpected Finding ◽  
Dna Ligases ◽  
Dna Ligase Iv ◽  
Human Dna ◽  
Dna Double Strand Break ◽  
Ligase Iv ◽  
Eukaryotic Dna ◽  
Catalytic Cycles

Abstract As nucleotidyl transferases, formation of a covalent enzyme-adenylate intermediate is a common first step of all DNA ligases. While it has been shown that eukaryotic DNA ligases utilize ATP as the adenylation donor, it was recently reported that human DNA ligase IV can also utilize NAD+ and, to a lesser extent ADP-ribose, as the source of the adenylate group and that NAD+, unlike ATP, enhances ligation by supporting multiple catalytic cycles. Since this unexpected finding has significant implications for our understanding of the mechanisms and regulation of DNA double strand break repair, we attempted to confirm that NAD+ and ADP-ribose can be used as co-factors by human DNA ligase IV. Here, we provide evidence that NAD+ does not enhance ligation by pre-adenylated DNA ligase IV, indicating that this co-factor is not utilized for re-adenylation and subsequent cycles of ligation. Moreover, we find that ligation by de-adenylated DNA ligase IV is dependent upon ATP not NAD+ or ADP-ribose. Thus, we conclude that human DNA ligase IV cannot use either NAD+ or ADP-ribose as adenylation donor for ligation.

scholarly journals SCR7 is neither a selective nor a potent inhibitor of human DNA ligase IV

DNA Repair ◽  
2016 ◽  
Vol 43 ◽  
pp. 18-23 ◽  
Author(s):  
George E. Greco ◽  
Yoshihiro Matsumoto ◽  
Rhys C. Brooks ◽  
Zhengfei Lu ◽  
Michael R. Lieber ◽  
...  
Keyword(s):  
Potent Inhibitor ◽  
Dna Ligase ◽  
Dna Ligase Iv ◽  
Human Dna ◽  
Ligase Iv

Late embryonic lethality and impaired V (D)J recombination in mice lacking DNA ligase IV

Nature ◽  
10.1038/24172 ◽  
1998 ◽  
Vol 396 (6707) ◽  
pp. 173-177 ◽  
Author(s):  
Karen M. Frank ◽  
JoAnn M. Sekiguchi ◽  
Katherine J. Seidl ◽  
Wojciech Swat ◽  
Gary A. Rathbun ◽  
...  
Keyword(s):  
Embryonic Lethality ◽  
Dna Ligase ◽  
Dna Ligase Iv ◽  
Ligase Iv

Absence of DNA ligase IV protein in XR-1 cells: evidence for stabilization by XRCC4

1999 ◽  
Vol 433 (1) ◽  
pp. 53-58 ◽  
Author(s):  
Margaret Bryans ◽  
Mary Carmen Valenzano ◽  
Thomas D. Stamato
Keyword(s):  
Dna Ligase ◽  
Dna Ligase Iv ◽  
Ligase Iv
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