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Human SLX4 Is a Holliday Junction Resolvase Subunit that Binds Multiple DNA Repair/Recombination Endonucleases
The Y-family of DNA polymerases.
Trading places: how do DNA polymerases switch during translesion DNA synthesis?
The dinB gene encodes a novel E. coli DNA polymerase, DNA pol IV, involved in mutagenesis.
All three SOS‐inducible DNA polymerases (Pol II, Pol IV and Pol V) are involved in induced mutagenesis
It is shown that, depending upon the nature of the DNA damage and its sequence context, the two additional SOS‐inducible DNA polymerases, Pol II (polB) and Pol IV (dinB), are also involved in error‐free and mutagenic translesion synthesis (TLS).
Co-localization in replication foci and interaction of human Y-family members, DNA polymerase pol eta and REVl protein.
How DNA lesions are turned into mutations within cells?
Recent aspects related to the genetics and biochemistry of TLS are presented and some of the remaining hot topics of this field are highlighted.
Molecular analysis of mutations in DNA polymerase η in xeroderma pigmentosum-variant patients
- B. Broughton, A. Cordonnier, A. Lehmann
- BiologyProceedings of the National Academy of Sciences…
- 2 January 2002
It is anticipated that protein in XP-V cells will not be localized in the nucleus nor will it be relocalized into replication foci during DNA replication, and the spectrum of both missense and truncating mutations is markedly skewed toward the N-terminal half of the protein.
Structural and biochemical analysis of sliding clamp/ligand interactions suggest a competition between replicative and translesion DNA polymerases.
Requirement of Rad5 for DNA Polymerase ζ-Dependent Translesion Synthesis in Saccharomyces cerevisiae
- Vincent Pagès, Anne Bresson, N. Acharya, S. Prakash, R. Fuchs, L. Prakash
- 1 September 2008
Evidence is provided for the requirement of Rad5 in TLS mediated by Polζ, and action in this role is likely to be structural, since neither the in activation of its ubiquitin ligase activity nor the inactivation of its helicase activity impairs its role in TLS.