scholarly journals Alternative Okazaki Fragment Ligation Pathway by DNA Ligase III

Genes ◽  
2015 ◽  
Vol 6 (2) ◽  
pp. 385-398 ◽  
Author(s):  
Hiroshi Arakawa ◽  
George Iliakis
Keyword(s):  
Dna Ligase ◽  
Okazaki Fragment ◽  
Dna Ligase Iii

scholarly journals An interaction between the mammalian DNA repair protein XRCC1 and DNA ligase III.

1994 ◽  
Vol 14 (1) ◽  
pp. 68-76 ◽  
Author(s):  
K W Caldecott ◽  
C K McKeown ◽  
J D Tucker ◽  
S Ljungquist ◽  
L H Thompson
Keyword(s):  
Dna Repair ◽  
Affinity Chromatography ◽  
Mammalian Cells ◽  
Excision Repair ◽  
Affinity Purification ◽  
Alkylating Agents ◽  
Chinese Hamster ◽  
Dna Ligase ◽  
Base Excision ◽  
Dna Ligase Iii

XRCC1, the human gene that fully corrects the Chinese hamster ovary DNA repair mutant EM9, encodes a protein involved in the rejoining of DNA single-strand breaks that arise following treatment with alkylating agents or ionizing radiation. In this study, a cDNA minigene encoding oligohistidine-tagged XRCC1 was constructed to facilitate affinity purification of the recombinant protein. This construct, designated pcD2EHX, fully corrected the EM9 phenotype of high sister chromatid exchange, indicating that the histidine tag was not detrimental to XRCC1 activity. Affinity chromatography of extract from EM9 cells transfected with pcD2EHX resulted in the copurification of histidine-tagged XRCC1 and DNA ligase III activity. Neither XRCC1 or DNA ligase III activity was purified during affinity chromatography of extract from EM9 cells transfected with pcD2EX, a cDNA minigene that encodes untagged XRCC1, or extract from wild-type AA8 or untransfected EM9 cells. The copurification of DNA ligase III activity with histidine-tagged XRCC1 suggests that the two proteins are present in the cell as a complex. Furthermore, DNA ligase III activity was present at lower levels in EM9 cells than in AA8 cells and was returned to normal levels in EM9 cells transfected with pcD2EHX or pcD2EX. These findings indicate that XRCC1 is required for normal levels of DNA ligase III activity, and they implicate a major role for this DNA ligase in DNA base excision repair in mammalian cells.

scholarly journals Human DNA Ligase III Recognizes DNA Ends by Dynamic Switching between Two DNA-Bound States

Biochemistry ◽  
2010 ◽  
Vol 49 (29) ◽  
pp. 6165-6176 ◽  
Author(s):  
Elizabeth Cotner-Gohara ◽  
In-Kwon Kim ◽  
Michal Hammel ◽  
John A. Tainer ◽  
Alan E. Tomkinson ◽  
...  
Keyword(s):  
Bound States ◽  
Dna Ligase ◽  
Dynamic Switching ◽  
Human Dna ◽  
Dna Ends ◽  
Dna Ligase Iii

scholarly journals Molecular cloning and expression of human cDNAs encoding a novel DNA ligase IV and DNA ligase III, an enzyme active in DNA repair and recombination.

1995 ◽  
Vol 15 (6) ◽  
pp. 3206-3216 ◽  
Author(s):  
Y F Wei ◽  
P Robins ◽  
K Carter ◽  
K Caldecott ◽  
D J Pappin ◽  
...  
Keyword(s):  
Dna Repair ◽  
Cdna Clone ◽  
Dna Ligase ◽  
Dna Ligases ◽  
Dna Ligase Iv ◽  
Ligase Iv ◽  
Dna Ligase I ◽  
Cloned Cdna ◽  
Dna Ligase Iii

Three distinct DNA ligases, I to III, have been found previously in mammalian cells, but a cloned cDNA has been identified only for DNA ligase I, an essential enzyme active in DNA replication. A short peptide sequence conserved close to the C terminus of all known eukaryotic DNA ligases was used to search for additional homologous sequences in human cDNA libraries. Two different incomplete cDNA clones that showed partial homology to the conserved peptide were identified. Full-length cDNAs were obtained and expressed by in vitro transcription and translation. The 103-kDa product of one cDNA clone formed a characteristic complex with the XRCC1 DNA repair protein and was identical with the previously described DNA ligase III. DNA ligase III appears closely related to the smaller DNA ligase II. The 96-kDa in vitro translation product of the second cDNA clone was also shown to be an ATP-dependent DNA ligase. A fourth DNA ligase (DNA ligase IV) has been purified from human cells and shown to be identical to the 96-kDa DNA ligase by unique agreement between mass spectrometry data on tryptic peptides from the purified enzyme and the predicted open reading frame of the cloned cDNA. The amino acid sequences of DNA ligases III and IV share a related active-site motif and several short regions of homology with DNA ligase I, other DNA ligases, and RNA capping enzymes. DNA ligases III and IV are encoded by distinct genes located on human chromosomes 17q11.2-12 and 13q33-34, respectively.

scholarly journals Involvement of XRCC1 and DNA Ligase III Gene Products in DNA Base Excision Repair

1997 ◽  
Vol 272 (38) ◽  
pp. 23970-23975 ◽  
Author(s):  
Enrico Cappelli ◽  
Richard Taylor ◽  
Michela Cevasco ◽  
Angelo Abbondandolo ◽  
Keith Caldecott ◽  
...  
Keyword(s):  
Base Excision Repair ◽  
Excision Repair ◽  
Dna Ligase ◽  
Gene Products ◽  
Dna Base Excision Repair ◽  
Dna Base ◽  
Base Excision ◽  
Dna Ligase Iii

scholarly journals Characterization of the XRCC1-DNA ligase III complexin vitroand its absence from mutant hamster cells

1995 ◽  
Vol 23 (23) ◽  
pp. 4836-4843 ◽  
Author(s):  
Keith W. Caldecott ◽  
James D. Tucker ◽  
Lawrence H. Stanker ◽  
Larry H. Thompson
Keyword(s):  
Dna Ligase ◽  
Dna Ligase Iii

scholarly journals A novel interaction between DNA ligase III and DNA polymerase γ plays an essential role in mitochondrial DNA stability

2007 ◽  
Vol 402 (1) ◽  
pp. 175-186 ◽  
Author(s):  
Ananya De ◽  
Colin Campbell
Keyword(s):  
Mitochondrial Dna ◽  
Dna Polymerase ◽  
Mitochondrial Protein ◽  
Dna Ligase ◽  
Zinc Finger Domain ◽  
Wild Type ◽  
Mitochondrial Dna Copy Number ◽  
Dna Polymerase Γ ◽  
Dna Ligase Iii

The data in the present study show that DNA polymerase γ and DNA ligase III interact in mitochondrial protein extracts from cultured HT1080 cells. An interaction was also observed between the two recombinant proteins in vitro. Expression of catalytically inert versions of DNA ligase III that bind DNA polymerase γ was associated with reduced mitochondrial DNA copy number and integrity. In contrast, overexpression of wild-type DNA ligase III had no effect on mitochondrial DNA copy number or integrity. Experiments revealed that wild-type DNA ligase III facilitates the interaction of DNA polymerase γ with a nicked DNA substrate in vitro, and that the zinc finger domain of DNA ligase III is required for this activity. Mitochondrial protein extracts prepared from cells overexpressing a DNA ligase III protein that lacked the zinc finger domain had reduced base excision repair activity compared with extracts from cells overexpressing the wild-type protein. These data support the interpretation that the interaction of DNA ligase III and DNA polymerase γ is required for proper maintenance of the mammalian mitochondrial genome.

scholarly journals Role of a BRCT domain in the interaction of DNA ligase III-α with the DNA repair protein XRCC1

1998 ◽  
Vol 8 (15) ◽  
pp. 877-880 ◽  
Author(s):  
Richard M. Taylor ◽  
Bill Wickstead ◽  
Sam Cronin ◽  
Keith W. Caldecott
Keyword(s):  
Dna Repair ◽  
Dna Ligase ◽  
Brct Domain ◽  
Repair Protein ◽  
Dna Repair Protein ◽  
Dna Ligase Iii
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