| Literature DB >> 19631767 |
Jennifer Yamtich1, Joann B Sweasy.
Abstract
The X family of DNA polymerases in eukaryotic cells consists of terminal transferase and DNA polymerases beta, lambda, and mu. These enzymes have similar structural portraits, yet different biochemical properties, especially in their interactions with DNA. None of these enzymes possesses a proofreading subdomain, and their intrinsic fidelity of DNA synthesis is much lower than that of a polymerase that functions in cellular DNA replication. In this review, we discuss the similarities and differences of three members of Family X: polymerases beta, lambda, and mu. We focus on biochemical mechanisms, structural variation, fidelity and lesion bypass mechanisms, and cellular roles. Remarkably, although these enzymes have similar three-dimensional structures, their biochemical properties and cellular functions differ in important ways that impact cellular function. Copyright (c) 2010 Elsevier B.V. All rights reserved.Entities:
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Year: 2009 PMID： 19631767 PMCID： PMC2846199 DOI： 10.1016/j.bbapap.2009.07.008
Source DB: PubMed Journal: Biochim Biophys Acta ISSN： 0006-3002