The cloning and characterization of a cDNA encoding Xenopus laevis DNA ligase I

Lepetit, David; Thiébaud, Pierre; Aoufouchi, Saïd; Prigent, Claude; Guesné, Rozène; Thézé, Nadine

doi:10.1016/0378-1119(96)00175-8

Cited by 5 publications

(3 citation statements)

References 15 publications

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“…The gel mobilities of molecular mass standards (in kilodaltons) are shown on the left. dant DNA ligase I (1,20) is not detected in the mitochondrial lysate. This provides the ideal control to indicate that the 100-kDa DNA ligase in the mitochondrial fraction is not a nuclear contaminant.…”

Section: Discussionmentioning

confidence: 86%

Efficient Repair of Abasic Sites in DNA by Mitochondrial Enzymes

Pinz

Bogenhagen

1998

Molecular and Cellular Biology

178

144

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Mutations in mitochondrial DNA (mtDNA) cause a variety of relatively rare human diseases and may contribute to the pathogenesis of other, more common degenerative diseases. This stimulates interest in the capacity of mitochondria to repair damage to mtDNA. Several recent studies have shown that some types of damage to mtDNA may be repaired, particularly if the lesions can be processed through a base excision mechanism that employs an abasic site as a common intermediate. In this paper, we demonstrate that a combination of enzymes purified from Xenopus laevis mitochondria efficiently repairs abasic sites in DNA. This repair pathway employs a mitochondrial class II apurinic/apyrimidinic (AP) endonuclease to cleave the DNA backbone on the 5 side of an abasic site. A deoxyribophosphodiesterase acts to remove the 5 sugar-phosphate residue left by AP endonuclease. mtDNA polymerase ␥ fills the resulting 1-nucleotide gap. The remaining nick is sealed by an mtDNA ligase. We report the first extensive purification of mtDNA ligase as a 100-kDa enzyme that functions with an enzyme-adenylate intermediate and is capable of ligating oligo(dT) strands annealed to poly(rA). These properties together with preliminary immunological evidence suggest that mtDNA may be related to nuclear DNA ligase III.

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Section: Discussionmentioning

confidence: 86%

Efficient Repair of Abasic Sites in DNA by Mitochondrial Enzymes

Pinz

Bogenhagen

1998

Molecular and Cellular Biology

178

144

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“…ATP-dependent DNA ligases, which are encoded by several viruses-including vaccinia virus, African swine fever virus (ASFV), and bacteriophages T3, T4, and T7-join two DNA fragments by catalyzing the formation of internucleotide phosphodiester bonds. They range in size from 268 amino acids in Haemophilus influenzae (17) to 1070 amino acids in Xenopus laevis (76). The 298-amino-acid-residue PBCV-1 enzyme, which is the second smallest DNA ligase described to date, has been expressed in E. coli, and the recombinant enzyme has been extensively characterized (53,(147)(148)(149).…”

Section: Similarities Of Pbcv-1 Open Reading Frames To Proteins In Thmentioning

confidence: 99%

Giant Viruses Infecting Algae

Etten

Meints

1999

Annu. Rev. Microbiol.

206

187

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Paramecium bursaria chlorella virus (PBCV-1) is the prototype of a family of large, icosahedral, plaque-forming, double-stranded-DNA-containing viruses that replicate in certain unicellular, eukaryotic chlorella-like green algae. DNA sequence analysis of its 330, 742-bp genome leads to the prediction that this phycodnavirus has 376 protein-encoding genes and 10 transfer RNA genes. The predicted gene products of approximately 40% of these genes resemble proteins of known function. The chlorella viruses have other features that distinguish them from most viruses, in addition to their large genome size. These features include the following: (a) The viruses encode multiple DNA methyltransferases and DNA site-specific endonucleases; (b) PBCV-1 encodes at least part, if not the entire machinery to glycosylate its proteins; (c) PBCV-1 has at least two types of introns--a self-splicing intron in a transcription factor-like gene and a splicesomal processed type of intron in its DNA polymerase gene. Unlike the chlorella viruses, large double-stranded-DNA-containing viruses that infect marine, filamentous brown algae have a circular genome and a lysogenic phase in their life cycle.

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“…3 B and 5 A). There is also considerable conservation (data not shown) with the Xenopus laevis DNA ligase I (25). The fact that the targeting sequence is missing or is very different in lower eukaryotic and prokaryotic DNA ligases and is also not required for complementation may indicate that it only recently developed in evolution.…”

Section: Mapping the Dna Ligase I Sequence Responsible For Targeting To Replication Focimentioning

confidence: 99%

Mapping and Use of a Sequence that Targets DNA Ligase I to Sites of DNA Replication In Vivo

Cardoso

Joseph

Rahn

et al. 1997

The Journal of Cell Biology

113

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The mammalian nucleus is highly organized, and nuclear processes such as DNA replication occur in discrete nuclear foci, a phenomenon often termed “functional organization” of the nucleus. We describe the identification and characterization of a bipartite targeting sequence (amino acids 1–28 and 111–179) that is necessary and sufficient to direct DNA ligase I to nuclear replication foci during S phase. This targeting sequence is located within the regulatory, NH2-terminal domain of the protein and is dispensable for enzyme activity in vitro but is required in vivo. The targeting domain functions position independently at either the NH2 or the COOH termini of heterologous proteins.We used the targeting sequence of DNA ligase I to visualize replication foci in vivo. Chimeric proteins with DNA ligase I and the green fluorescent protein localized at replication foci in living mammalian cells and thus show that these subnuclear functional domains, previously observed in fixed cells, exist in vivo. The characteristic redistribution of these chimeric proteins makes them unique markers for cell cycle studies to directly monitor entry into S phase in living cells.

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The cloning and characterization of a cDNA encoding Xenopus laevis DNA ligase I

Cited by 5 publications

References 15 publications

Efficient Repair of Abasic Sites in DNA by Mitochondrial Enzymes

Efficient Repair of Abasic Sites in DNA by Mitochondrial Enzymes

Giant Viruses Infecting Algae

Mapping and Use of a Sequence that Targets DNA Ligase I to Sites of DNA Replication In Vivo

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