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

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

The BRCT domain (for BRCA1 carboxyl terminus) is a protein motif of unknown function, comprising approximately 100 amino acids in five conserved blocks denoted A–E. BRCT domains are present in the tumour suppressor protein BRCA1 [1—3], and the domain is found in over 40 other proteins, defining a superfamily that includes DNA ligase III-a and the essential human DNA repair protein XRCC1. DNA li...

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HSP90 regulates DNA repair via the interaction between XRCC1 and DNA polymerase β

Cellular DNA repair processes are crucial to maintain genome stability and integrity. In DNA base excision repair, a tight heterodimer complex formed by DNA polymerase β (Polβ) and XRCC1 is thought to facilitate repair by recruiting Polβ to DNA damage sites. Here we show that disruption of the complex does not impact DNA damage response or DNA repair. Instead, the heterodimer formation is requi...

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Mitochondrial DNA ligase III function is independent of Xrcc1.

Hamster EM9 cells, which lack Xrcc1 protein, have reduced levels of DNA ligase III and are defective in nuclear base excision repair. The Xrcc1 protein stabilizes DNA ligase III and may even play a direct role in catalyzing base excision repair. Since DNA ligase III is also thought to function in mitochondrial base excision repair, it seemed likely that mitochondrial DNA ligase III function wou...

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A novel interaction between DNA ligase III and DNA polymerase gamma plays an essential role in mitochondrial DNA stability.

The data in the present study show that DNA polymerase gamma 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 gamma was associated with reduced mitochondrial DNA copy number and integrity. I...

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Mammalian DNA double-strand break repair protein XRCC4 interacts with DNA ligase IV

BACKGROUND Mammalian cells deficient in the XRCC4 DNA repair protein are impaired in DNA double-strand break repair and are consequently hypersensitive to ionising radiation. These cells are also defective in site-specific V(D)J recombination, a process that generates the diversity of antigen receptor genes in the developing immune system. These features are shared by cells lacking components o...

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ژورنال

عنوان ژورنال: Molecular and Cellular Biology

سال: 1994

ISSN: 0270-7306,1098-5549

DOI: 10.1128/mcb.14.1.68