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Publication Abstract from PubMed

The Y-family polymerases help cells tolerate DNA damage by performing translesion synthesis, yet they also can be highly error-prone. One distinctive feature of the DinB class of Y-family polymerases is that they make single-base deletion errors at high frequencies in repetitive sequences, especially those that contain two or more identical pyrimidines with a 5' flanking guanosine. Intriguingly, different deletion mechanisms have been proposed even for two archaeal DinB polymerases that share 54% sequence identity and originate from two strains of Sulfolobus. To reconcile these apparent differences, we have characterized Dpo4 from S. solfataricus using the same biochemical and crystallographic approaches that we have used previously to characterize Dbh from S. acidocaldarius. In contrast to previous suggestions that Dpo4 uses a dNTP-stabilized misalignment mechanism when creating single-base deletions, we find that Dpo4 predominantly uses a template-slippage deletion mechanism when replicating repetitive DNA sequences, as was previously shown for Dbh. Dpo4 stabilizes the skipped template base in an extrahelical conformation between the polymerase and the little-finger domains of the enzyme. This contrasts with Dbh, where the extrahelical base is stabilized against the surface of little-finger domain alone. Thus, despite sharing a common deletion mechanism, these closely related polymerases use different contacts with the substrate to accomplish the same result.

The Y-family DNA polymerase Dpo4 uses a template-slippage mechanism to create single-base deletions.,Wu Y, Wilson RC, Pata JD J Bacteriol. 2011 Mar 18. PMID:21421759^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.