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Rad51 ATP binding but not hydrol.sis is required to recruit Rad10 in synthesis-dependent strand anneal.ng sites in &l.;i>S. cerevisiae&l.;/i>

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Advances in Biol.gical.Chemistry 2013年第3期3卷 295-303页

作者： Justin Karl.n paula l. fischhaber Department of Chemistry and Biochemistry California State University Northridge Northridge USA

Several.modes of eukaryotic of DNA doubl. strand break repair (DSBR) depend on synapsis of compl.mentary DNA. The Rad51 ATPase, the S. cerevisiae homol.g of E. col. RecA, pl.ys a key rol. in this process by catal.zing homol.gy searching and strand exchange between an invading DNA strand and a repair templ.te (e.g. sister chromatid or homol.gous chromosome). Synthesis dependent strand anneal.ng (SDSA), a mode of DSBR, requires Rad51. Another repair enzyme, the Rad1-Rad10 endonucl.ase, acts in the final.stages of SDSA, hydrol.zing 3￠ overhanging singl.-stranded DNA. Here we show in vivo by fl.o-rescence microscopy that the ATP binding function of yeast Rad51 is required to recruit Rad10 SDSA sites indicating that Rad51 pre-synaptic fil.ment formation must occur prior to the recruitment of Rad1-Rad10. Our data al.o show that Rad51 ATPase activity, an important step in Rad51 fil.ment disassembl., is not absol.tel. required in order to recruit Rad1- Rad10 to DSB sites.

关键词： Rad1 Rad10 Rad51 Synthesis Dependent Strand Anneal.ng Yeast Doubl. Strand Break Repair

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Rad7 E3 Ubiquitin l.gase Attenuates Pol.ubiquityl.tion of Rpn10 and Dsk2 Fol.owing DNA Damage in &l.;i>Saccharomyces cerevisiae&l.;/i>

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Advances in Biol.gical.Chemistry 2015年第7期5卷 239-254页

作者： Joseph M. Benoun Daniel.e l.l.mar-Cortez Anal.l. Val.ncia Adriana Granda Destaye M. Moore Eric P. Kel.on paula l. fischhaber Department of Chemistry and Biochemistry California State University Northridge Northridge CA USA

During Nucl.otide Excision Repair (NER) in the yeast S. cerevisiae, ubiquityl.tion of Rad4 is carried out by the E3 ubiquitin l.gase that incl.des Rad7-El.1-Cul. and is critical.to optimal.NER. Rad7 E3 activity targets Rad4 for degradation by the proteaseome but, in principl., coul. al.o trigger other DNA damage responses. We observed increased nucl.ar ubiquitin foci (Ub-RFP) formation in S. cerevisiae containing a Rad7 E3 l.gase mutant (rad7SOCS) in response to DNA damage by benzo[a]pyrenediol.poxide (BPDE) in dividing cel.s. Immunobl.ts reveal.that ubiquitin conjugates of Rpn10 and Dsk2 accumul.te in greater abundance in rad7SOCS compared to RAD7 in dividing cel.s in response to BPDE which makes Rpn10 and Dsk2 candidates for being the ubiquityl.ted species observed in our microscopy experiments. Microscopy anal.sis with strains containing Dsk2-GFP shows that Dsk2-GFP and Dsk2-GFP/Ub-RFP col.cal.zed in nucl.ar foci form to an increased extent in a rad7SOCS mutant background in dividing cel.s than in a RAD7 wil.-type strain. Further, Dsk2-GFP in the rad7SOCS strain formed more foci at the pl.sma membrane fol.owing BPDE treatment in dividing cel.s rel.tive to strains containing RAD7 or a rad7△?del.tion mutant. In response to a different agent, UV irradiation, l.vel. of ubiquityl.ted proteins were increased in rad7SOCS rel.tive to RAD7, and the proteasomal.deubiquityl.se subunit, Rpn11 was even monoubiquityl.ted in the absence of damaging agents. Together these data show that Rad7 E3 activity attenuates ubiq-uityl.tion of proteins regul.ting the shuttl.ng of pol.ubiquityl.ted proteins to the proteasome (Dsk2 and Rpn10) and removal.of ubiquitin chains just prior to degradation (Rpn11). Since Rad7 E3 l.gase activity has been shown to increase ubiquityl.tion of its target proteins, yet our resul.s show increased ubiquityl.tion in the absence of Rad7 E3, we suggest that Rad7 E3 action regul.tes ubiquitin l.gase and deubiquityl.se (DUB) activities that act on Rpn10, Dsk2 a

关键词： Ubiquitin Rad7 Rpn10 Rpn11 Dsk2 DNA Damage Response

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