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Recent Advances in Understanding the Structures of Translesion Synthesis DNA Polymerases
Journal article   Open access   Peer reviewed

Recent Advances in Understanding the Structures of Translesion Synthesis DNA Polymerases

Justin A Ling, Zach Frevert and M Todd Washington
Genes, Vol.13(5), p.915
05/20/2022
DOI: 10.3390/genes13050915
PMCID: PMC9141541
PMID: 35627300
url
https://doi.org/10.3390/genes13050915View
Published (Version of record) Open Access

Abstract

DNA damage in the template strand causes replication forks to stall because replicative DNA polymerases are unable to efficiently incorporate nucleotides opposite template DNA lesions. To overcome these replication blocks, cells are equipped with multiple translesion synthesis polymerases that have evolved specifically to incorporate nucleotides opposite DNA lesions. Over the past two decades, X-ray crystallography has provided a wealth of information about the structures and mechanisms of translesion synthesis polymerases. This approach, however, has been limited to ground state structures of these polymerases bound to DNA and nucleotide substrates. Three recent methodological developments have extended our understanding of the structures and mechanisms of these polymerases. These include time-lapse X-ray crystallography, which allows one to identify novel reaction intermediates; full-ensemble hybrid methods, which allow one to examine the conformational flexibility of the intrinsically disordered regions of proteins; and cryo-electron microscopy, which allows one to determine the high-resolution structures of larger protein complexes. In this article, we will discuss how these three methodological developments have added to our understanding of the structures and mechanisms of translesion synthesis polymerases.
 Cryoelectron Microscopy DNA - genetics DNA Replication DNA-Directed DNA Polymerase - genetics Nucleotides

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