Human DNA Polymerase beta, but Not lambda, Can Bypass a 2-Deoxyribonolactone Lesion Together with Proliferating Cell Nuclear Antigen (Articolo in rivista)

Type
Label
  • Human DNA Polymerase beta, but Not lambda, Can Bypass a 2-Deoxyribonolactone Lesion Together with Proliferating Cell Nuclear Antigen (Articolo in rivista) (literal)
Anno
  • 2013-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1021/cb300542k (literal)
Alternative label
  • Crespan E, Pasi E, Imoto S, Hubscher U, Greenberg MM, Maga G (2013)
    Human DNA Polymerase beta, but Not lambda, Can Bypass a 2-Deoxyribonolactone Lesion Together with Proliferating Cell Nuclear Antigen
    in ACS chemical biology
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Crespan E, Pasi E, Imoto S, Hubscher U, Greenberg MM, Maga G (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#altreInformazioni
  • in press (literal)
Rivista
Note
  • ubMe (literal)
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Institute of Molecular Genetics IGM-CNR, via Abbiategrasso 207, I-27100 Pavia, Italy; Department of Chemistry, Johns Hopkins University, 3400 N. Charles St., Baltimore, Maryland 21218, United States; Institute of Veterinary Biochemistry and Molecular Biology, University of Zurich-Irchel, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland (literal)
Titolo
  • Human DNA Polymerase beta, but Not lambda, Can Bypass a 2-Deoxyribonolactone Lesion Together with Proliferating Cell Nuclear Antigen (literal)
Abstract
  • The C1'-oxidized lesion 2-deoxyribonolactone (L) is induced by free radical attack of DNA. This lesion is mutagenic, inhibits base excision repair, and can lead to strand scission. In double-stranded DNA L is repaired by long-patch base excision repair, but it induces replication fork arrest in a single-strand template. Translesion synthesis requires a specialized DNA polymerase (Pol). In E. coli, Pol V is responsible for bypassing L, whereas in yeast Pol zeta has been shown to be required for efficient bypass. Very little is known about the identity of human Pols capable of bypassing L. For instance, the activity of family X enzymes has never been investigated. We examined the ability of different family X Pols: Pols beta, lambda, and TdT from human cells and Pol IV from S. cerevisiae to act on DNA containing an isolated 2-deoxyribonolactone, as well as when the lesion comprises the 5'-component of a tandem lesion. We show that Pol beta, but not Pol lambda, can bypass a single L lesion in the template, and its activity is increased by the auxiliary protein proliferating cell nuclear antigen (PCNA), whereas both enzymes were completely blocked by a tandem lesion. Yeast Pol IV was able to bypass the single L and the tandem lesion but with little nucleotide insertion specificity. Finally, L did not affect the polymerization activity of the template-independent enzyme TdT. (literal)
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