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Science 16 December 2005:
Vol. 310. no. 5755, p. 1737
DOI: 10.1126/science.310.5755.1737m
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This Week in Science
The main replicative DNA polymerase has evolved to recognize DNA with high fidelity, but this capability also makes it very poor at dealing with damaged DNA, where it very often stalls at the point of damage. A series of "damage-specific" DNA polymerases that can handle distorted or abasic templates are recruited to the stalled polymerase partly through the ubiquitinylation of proliferating cell nuclear antigen (PCNA)--but how this occurs has been a mystery. Bienko et al. (p. 1821) now show that all the Y-family damage-specific translesion synthesis (TLS) polymerases contain two previously undetected types of ubiquitin binding domain. Colocalization of two TLS polymerases with PCNA in replication factories depends on these ubiquitin binding domains, as do the ability to interact with ubiquitinylated-PCNA and the ability to facilitate DNA repair.
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Science. ISSN 0036-8075 (print), 1095-9203 (online)
