2008
Wrestling SUMO on proteins involved in homologous recombination
ALTMANNOVÁ, Veronika a Lumír KREJČÍZákladní údaje
Originální název
Wrestling SUMO on proteins involved in homologous recombination
Název česky
SUMO a proteiny účastnící se homologní rekombinace
Název anglicky
Wrestling SUMO on proteins involved in homologous recombination
Autoři
ALTMANNOVÁ, Veronika a Lumír KREJČÍ
Vydání
2008
Další údaje
Jazyk
čeština
Typ výsledku
Audiovizuální tvorba
Obor
10600 1.6 Biological sciences
Stát vydavatele
Rakousko
Utajení
není předmětem státního či obchodního tajemství
Odkazy
Organizační jednotka
Přírodovědecká fakulta
Klíčová slova anglicky
SUMOylation; homologous recombination
Štítky
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.
Anglicky
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.
Návaznosti
ME 888, projekt VaV |
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MSM0021622413, záměr |
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