| Literature DB >> 17874115 |
Ritu Pabla1, Donald Rozario, Wolfram Siede.
Abstract
RAD30-encoded DNA polymerase eta functions as a translesion polymerase that can bypass the most frequent types of UV-induced pyrimidine photoproducts in an error-free manner. Although its transcript is UV-inducible in Saccharomyces cerevisiae, Rad30 (studied as a Rad30-Myc fusion) is a stable protein whose levels do not fluctuate following UV treatment or during cell cycle progression. Rad30 protein is subject to monoubiquitination whose level is upregulated in G1 and downregulated during S-phase reentry. This downregulation is accelerated in UV-treated cells. A missense mutation (L577Q) of the ubiquitin binding domain (UBZ) confers a reduced degree of ubiquitination outside of G1 and a complete failure to stably interact with ubiquitinated substrates. This mutation confers a phenotype resembling a complete RAD30 deletion, thus attesting to the significance of the UBZ motif for polymerase eta function in vivo.Entities:
Mesh:
Substances:
Year: 2007 PMID: 17874115 DOI: 10.1007/s00411-007-0132-1
Source DB: PubMed Journal: Radiat Environ Biophys ISSN: 0301-634X Impact factor: 1.925