Detailed Information on Publication Record
2008
Wrestling SUMO on proteins involved in homologous recombination
ALTMANNOVÁ, Veronika and Lumír KREJČÍBasic information
Original name
Wrestling SUMO on proteins involved in homologous recombination
Name in Czech
SUMO a proteiny účastnící se homologní rekombinace
Name (in English)
Wrestling SUMO on proteins involved in homologous recombination
Authors
ALTMANNOVÁ, Veronika and Lumír KREJČÍ
Edition
2008
Other information
Language
Czech
Type of outcome
Audiovizuální tvorba
Field of Study
10600 1.6 Biological sciences
Country of publisher
Austria
Confidentiality degree
není předmětem státního či obchodního tajemství
References:
Organization unit
Faculty of Science
Keywords in English
SUMOylation; homologous recombination
Změněno: 14/11/2008 21:42, Mgr. Veronika Altmannová, Ph.D.
V originále
Homologous recombination (HR) is a process widespread in nature and essential to maintain the integrity of the genome via repair of DNA double-strand breaks (DSBs). Rad52 is a DNA-binding protein which plays a key role in HR. It mediates the exchange of the recombination factor RPA associated to single-stranded DNA (ssDNA) by Rad51, resulting in the assembly of the presynaptic filament. Recently, it has been reported that upon DNA damage Rad52 is modified by the small ubiquitin-like modifier (SUMO) protein which shelters Rad52 against proteosomal degradation. As the major SUMOylation sites of Rad52, three lysines (K43, K44, K253) have been identified. The effect of Rad52 DNA binding and interaction with its partners was tested to clarify the regulatory mechanism of Rad52 SUMOylation.
In English
Homologous recombination (HR) is a process widespread in nature and essential to maintain the integrity of the genome via repair of DNA double-strand breaks (DSBs). Rad52 is a DNA-binding protein which plays a key role in HR. It mediates the exchange of the recombination factor RPA associated to single-stranded DNA (ssDNA) by Rad51, resulting in the assembly of the presynaptic filament. Recently, it has been reported that upon DNA damage Rad52 is modified by the small ubiquitin-like modifier (SUMO) protein which shelters Rad52 against proteosomal degradation. As the major SUMOylation sites of Rad52, three lysines (K43, K44, K253) have been identified. The effect of Rad52 DNA binding and interaction with its partners was tested to clarify the regulatory mechanism of Rad52 SUMOylation.
Links
| ME 888, research and development project |
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| MSM0021622413, plan (intention) |
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