| Literature DB >> 24076078 |
Fernanda Mosena Munari1, Temenouga Nikolova Guecheva, Diego Bonatto, João Antônio Pêgas Henriques.
Abstract
Pso2 protein, a member of the highly conserved metallo-β-lactamase (MBL) super family of nucleases, plays a central role in interstrand crosslink repair (ICL) in yeast. Pso2 protein is the founder member of a distinct group within the MBL superfamily, called β-CASP family. Three mammalian orthologs of this protein that act on DNA were identified: SNM1A, SNM1B/Apollo and SNM1C/Artemis. Yeast Pso2 and all three mammalian orthologs proteins have been shown to possess nuclease activity. Besides Pso2, ICL repair involves proteins of several DNA repair pathways. Over the last years, new homologs for human proteins have been identified in yeast. In this review, we will focus on studies clarifying the function of Pso2 protein during ICL repair in yeast, emphasizing the contribution of Brazilian research groups in this topic. New sub-pathways in the mechanisms of ICL repair, such as recently identified conserved Fanconi Anemia pathway in yeast as well as a contribution of non-homologous end joining are discussed.Entities:
Keywords: 8-Methoxypsoralen; Bifunctional chemotherapeutic drugs; DNA interstrand crosslink repair; Double strand breaks; PSO2/SNM1; Saccharomyces cerevisiae
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Year: 2013 PMID: 24076078 DOI: 10.1016/j.fgb.2013.09.003
Source DB: PubMed Journal: Fungal Genet Biol ISSN: 1087-1845 Impact factor: 3.495