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Results for “Exonucleases”

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PubMed2004

Replication factors license exonuclease I in mismatch repair.

A key question in the eukaryotic mismatch repair field is how strand excision is coordinated with mismatch recognition. In a recent issue of Molecular Cell, Dzantiev et al. present evidence that the replication factors PCNA and RFC modulate the directionality of EXOI-mediated excision.

Animals↗
PubMed2003

Investigation of the role of the histidine-aspartate pair in the human exonuclease III-like abasic endonuclease, Ape1.

Hydrogen bonded histidine-aspartate (His-Asp) pairs are critical constituents in several key enzymatic reactions. To date, the role that these pairs play in catalysis is best understood in serine and trypsin-like proteases, where structural and biochemical NMR studies have revealed important pK(a) values and hydrogen bonding patterns within the catalytic pocket. However, the role of the His-Asp pair in metal-assisted catalysis is less clear. Here, we apply liquid-state NMR to investigate the role of a critical histidine residue of apurinic endonuclease 1 (Ape1), a human DNA repair enzyme that cleaves adjacent to abasic sites in DNA using one or more divalent cations and an active-site His-Asp pair. The results of these studies suggest that the Ape1 His-Asp pair does not function as either a general base catalyst or a metal ligand. Rather, the pair likely stabilizes the pentavalent transition state necessary for phospho-transfer.

Aspartic Acid↗