XRCC1 protein interacts with one of two distinct forms of DNA ligase III.

作者: Rachel A. Nash , Keith W. Caldecott , Deborah E. Barnes , Tomas Lindahl

DOI: 10.1021/BI962281M

关键词:

摘要: Human DNA ligase III (103 kDa) has been shown to interact directly with the 70 kDa repair protein, XRCC1. Here, binding sites have defined. Subcloned fragments of XRCC1 expressed and assayed for their ability associate by far Western affinity precipitation analyses. The C-terminal 96 amino acids are necessary sufficient specific interaction III. A similar approach 103 identified 148 this enzyme as containing site An alternative form III, abundant in testes, described [Chen, J., et al. (1995) Mol. Cell. Biol. 15, 5412-5422]. These two forms identical N-terminal regions but differ toward C termini may be alternatively spliced products same gene. Antipeptide antibodies directed against different indicate that both them occur vivo. region derivative is not able findings only larger acts together XRCC1, suggesting a role isoform base excision repair.

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