Yeast DNA polymerase η possesses two PIP-like motifs that bind PCNA and Rad6-Rad18 with different specificities
- 6 September 2020
- journal article
- research article
- Published by Elsevier in DNA Repair
- Vol. 95, 102968
Abstract
No abstract availableKeywords
Funding Information
- National Institute of General Medical Sciences (GM081433)
This publication has 56 references indexed in Scilit:
- Readers of PCNA modificationsChromosoma, 2013
- A non-catalytic role of DNA polymerase η in recruiting Rad18 and promoting PCNA monoubiquitination at stalled replication forksNucleic Acids Research, 2013
- Regulation of the specialized DNA polymerase eta: Revisiting the biological relevance of its PCNA‐ and ubiquitin‐binding motifsEnvironmental and Molecular Mutagenesis, 2012
- Y-family DNA polymerases and their role in tolerance of cellular DNA damageNature Reviews Molecular Cell Biology, 2012
- Variations on a theme: Eukaryotic Y-family DNA polymerasesBiochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2009
- Structural Basis for Novel Interactions between Human Translesion Synthesis Polymerases and Proliferating Cell Nuclear AntigenJournal of Biological Chemistry, 2009
- Eukaryotic Translesion Polymerases and Their Roles and Regulation in DNA Damage ToleranceMicrobiology and Molecular Biology Reviews, 2009
- Functional characterization of Rad18 domains for Rad6, ubiquitin, DNA binding and PCNA modificationNucleic Acids Research, 2007
- RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMONature, 2002
- Structure of the C-Terminal Region of p21WAF1/CIP1 Complexed with Human PCNACell, 1996