English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/133183
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE
Exportar a otros formatos:


Alternative solutions and new scenarios for translesion DNA synthesis by human PrimPol

AuthorsMartínez-Jiménez, María I. CSIC ORCID ; García-Gómez, Sara CSIC; Bebenek, Katarzyna; Sastre-Moreno, Guillermo; Calvo, Patricia A.; Díaz-Talavera, Alberto CSIC; Kunkel, Thomas A.; Blanco, Luis CSIC ORCID
Translesion synthesisa
Lesion bypass
DNA polymerase
DNA Primase
Issue Date23-Feb-2015
CitationDNA Repair 29: 127- 138 (2015)
Abstract© 2015 Elsevier B.V. PrimPol is a recently described DNA polymerase that has the virtue of initiating DNA synthesis. In addition of being a sensu stricto DNA primase, PrimPol's polymerase activity has a large capacity to tolerate different kind of lesions. The different strategies used by PrimPol for DNA damage tolerance are based on its capacity to >read> certain lesions, to skip unreadable lesions, and as an ultimate solution, to restart DNA synthesis beyond the lesion thus acting as a TLS primase. This lesion bypass potential, revised in this article, is strengthened by the preferential use of moderate concentrations of manganese ions as the preferred metal activator. We show here that PrimPol is able to extend RNA primers with ribonucleotides, even when bypassing 8oxoG lesions, suggesting a potential new scenario for PrimPol as a TLS polymerase assisting transcription. We also show that PrimPol displays a high degree of versatility to accept or induce distortions of both primer and template strands, creating alternative alignments based on microhomology that would serve to skip unreadable lesions and to connect separate strands. In good agreement, PrimPol is highly prone to generate indels at short nucleotide repeats. Finally, an evolutionary view of the relationship between translesion synthesis and primase functions is briefly discussed.
Identifiersdoi: 10.1016/j.dnarep.2015.02.013
issn: 1568-7856
Appears in Collections:(CBM) Artículos
Files in This Item:
File Description SizeFormat 
Blanco L Alternative solutions.pdf2,28 MBAdobe PDFThumbnail
Show full item record
Review this work

Related articles:

WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.