SARANGI, Prabha, Zdenka BARTOŠOVÁ, Veronika ALTMANNOVÁ, Cory HOLLAND, Melita CHAVDAROVA, Sang Eun LEE, Lumír KREJČÍ a Xiaolan ZHAO. Sumoylation of the Rad1 nuclease promotes DNA repair and regulates its DNA association. Nucleic Acids Research. Oxford University Press, 2014, roč. 42, č. 10, s. 6393-6404. ISSN 0305-1048. Dostupné z: https://dx.doi.org/10.1093/nar/gku300. |
Další formáty:
BibTeX
LaTeX
RIS
@article{1184062, author = {Sarangi, Prabha and Bartošová, Zdenka and Altmannová, Veronika and Holland, Cory and Chavdarova, Melita and Lee, Sang Eun and Krejčí, Lumír and Zhao, Xiaolan}, article_number = {10}, doi = {http://dx.doi.org/10.1093/nar/gku300}, keywords = {NUCLEOTIDE EXCISION-REPAIR; TRANSCRIPTION FACTOR TFIIH; SACCHAROMYCES-CEREVISIAE; IN-VIVO; HOMOLOGOUS RECOMBINATION; BUDDING YEAST; RAD1-RAD10 NUCLEASE; DAMAGE RECOGNITION; SUMO MODIFICATION; STRAND BREAKS}, language = {eng}, issn = {0305-1048}, journal = {Nucleic Acids Research}, title = {Sumoylation of the Rad1 nuclease promotes DNA repair and regulates its DNA association}, volume = {42}, year = {2014} }
TY - JOUR ID - 1184062 AU - Sarangi, Prabha - Bartošová, Zdenka - Altmannová, Veronika - Holland, Cory - Chavdarova, Melita - Lee, Sang Eun - Krejčí, Lumír - Zhao, Xiaolan PY - 2014 TI - Sumoylation of the Rad1 nuclease promotes DNA repair and regulates its DNA association JF - Nucleic Acids Research VL - 42 IS - 10 SP - 6393-6404 EP - 6393-6404 PB - Oxford University Press SN - 03051048 KW - NUCLEOTIDE EXCISION-REPAIR KW - TRANSCRIPTION FACTOR TFIIH KW - SACCHAROMYCES-CEREVISIAE KW - IN-VIVO KW - HOMOLOGOUS RECOMBINATION KW - BUDDING YEAST KW - RAD1-RAD10 NUCLEASE KW - DAMAGE RECOGNITION KW - SUMO MODIFICATION KW - STRAND BREAKS N2 - The Saccharomyces cerevisiae Rad1-Rad10 complex is a conserved, structure-specific endonuclease important for repairing multiple types of DNA lesions. Upon recruitment to lesion sites, Rad1-Rad10 removes damaged sequences, enabling subsequent gap filling and ligation. Acting at mid-steps of repair, the association and dissociation of Rad1-Rad10 with DNA can influence repair efficiency. We show that genotoxin-enhanced Rad1 sumoylation occurs after the nuclease is recruited to lesion sites. A single lysine outside Rad1's nuclease and Rad10-binding domains is sumoylated in vivo and in vitro. Mutation of this site to arginine abolishes Rad1 sumoylation and impairs Rad1-mediated repair at high doses of DNA damage, but sustains the repair of a single double-stranded break. The timing of Rad1 sumoylation and the phenotype bias toward high lesion loads point to a post-incision role for sumoylation, possibly affecting Rad1 dissociation from DNA. Indeed, biochemical examination shows that sumoylation of Rad1 decreases the complex's affinity for DNA without affecting other protein properties. These findings suggest a model whereby sumoylation of Rad1 promotes its disengagement from DNA after nuclease cleavage, allowing it to efficiently attend to large numbers of DNA lesions. ER -
SARANGI, Prabha, Zdenka BARTOŠOVÁ, Veronika ALTMANNOVÁ, Cory HOLLAND, Melita CHAVDAROVA, Sang Eun LEE, Lumír KREJČÍ a Xiaolan ZHAO. Sumoylation of the Rad1 nuclease promotes DNA repair and regulates its DNA association. \textit{Nucleic Acids Research}. Oxford University Press, 2014, roč.~42, č.~10, s.~6393-6404. ISSN~0305-1048. Dostupné z: https://dx.doi.org/10.1093/nar/gku300.
|