Rad52 sumoylation affects the efficiency of the recombination and repair

KREJČÍ, Lumír. Rad52 sumoylation affects the efficiency of the recombination and repair. Kréta, Řecko: DNA Repair, 2009.

Basic information

• Original name: Rad52 sumoylation affects the efficiency of the recombination and repair
• Name in Czech: SUMOylace Rad52 proteinu ovlivnuje ucinnost rekombinace a DNA opravy
• Authors: KREJČÍ, Lumír.
• Edition: Kréta, Řecko, 2009.
• Publisher: DNA Repair

Other information

• Original language: English
• Type of outcome: Audiovisual works
• Field of Study: 10600 1.6 Biological sciences
• Country of publisher: Italy
• Confidentiality degree: is not subject to a state or trade secret
• WWW: URL
• Organization unit: Faculty of Medicine
• Keywords in English: DNA repair; DNA damage; replication; genomic instability
• Tags: DNA damage, DNA repair, genomic instability, replication
• Tags: International impact

Abstract

Homologous recombination (HR) plays a vital role in DNA metabolic processes including meiosis, DNA repair, DNA replication, and maintenance of rDNA homeostasis. Defects in HR can lead to pathological outcomes, including genetic diseases and cancer. Recent studies suggest that the post-translational modification by small ubiquitin-like modifier (SUMO) protein plays an important role in mitotic and meiotic recombination. We find that SUMOylation can significantly influence the biochemical properties of the modified proteins as well as their localization. The precise role of SUMOylation during recombination and DNA repair is still indistinct. Characterization of the novel effect of SUMOylation on the properties of Saccharomyces cerevisiae mediator protein Rad52 will be presented and the model for the recombination quality control discussed.

Abstract (in Czech)

Homologous recombination (HR) plays a vital role in DNA metabolic processes including meiosis, DNA repair, DNA replication, and maintenance of rDNA homeostasis. Defects in HR can lead to pathological outcomes, including genetic diseases and cancer. Recent studies suggest that the post-translational modification by small ubiquitin-like modifier (SUMO) protein plays an important role in mitotic and meiotic recombination. We find that SUMOylation can significantly influence the biochemical properties of the modified proteins as well as their localization. The precise role of SUMOylation during recombination and DNA repair is still indistinct. Characterization of the novel effect of SUMOylation on the properties of Saccharomyces cerevisiae mediator protein Rad52 will be presented and the model for the recombination quality control discussed.

Links

• GA301/09/1917, research and development project: Name: Štěpení replikačních-rekombinačních DNA meziproduktů a jejich úloha při nestabilitě genomu

Investor: Czech Science Foundation

• GD203/09/H046, research and development project: Name: Biochemie na rozcestí mezi in silico a in vitro

Investor: Czech Science Foundation

• LC06030, research and development project: Name: Biomolekulární centrum

Investor: Ministry of Education, Youth and Sports of the CR, Biomolecular centre

• MSM0021622413, plan (intention): Name: Proteiny v metabolismu a při interakci organismů s prostředím

Investor: Ministry of Education, Youth and Sports of the CR, Proteins in metabolism and interaction of organisms with the environment