| Bre1/RNF20 promotes Rad51-mediated strand exchange and antagonizes the Srs2/FBH1 helicases. | Bre1/RNF20 promotes Rad51-mediated strand exchange and antagonizes the Srs2/FBH1 helicases.
Liu G, Li J, He B, Yan J, Zhao J, Wang X, Zhao X, Xu J, Wu Y, Zhang S, Gan X, Zhou C, Li X, Zhang X, Chen X., Free PMC Article | 06/12/2023 |
| Genetic Dissection of Budding Yeast PCNA Mutations Responsible for the Regulated Recruitment of Srs2 Helicase. | Genetic Dissection of Budding Yeast PCNA Mutations Responsible for the Regulated Recruitment of Srs2 Helicase.
Fan L, Zhang W, Rybchuk J, Luo Y, Xiao W., Free PMC Article | 04/28/2023 |
| Rad54 and Rdh54 prevent Srs2-mediated disruption of Rad51 presynaptic filaments. | Rad54 and Rdh54 prevent Srs2-mediated disruption of Rad51 presynaptic filaments.
Meir A, Crickard JB, Kwon Y, Sung P, Greene EC., Free PMC Article | 03/5/2022 |
| Prevention of unwanted recombination at damaged replication forks. | Prevention of unwanted recombination at damaged replication forks.
Lehmann CP, Jiménez-Martín A, Branzei D, Tercero JA., Free PMC Article | 06/5/2021 |
| Srs2 C-terminal Rad51 interaction domain is essential for crossover control in S. cerevisiae. | Role of the Srs2-Rad51 Interaction Domain in Crossover Control in Saccharomyces cerevisiae.
Jenkins SS, Gore S, Guo X, Liu J, Ede C, Veaute X, Jinks-Robertson S, Kowalczykowski SC, Heyer WD., Free PMC Article | 01/25/2020 |
| DNA helicase domain of Saccharomyces cerevisiae yeast Srs2 protein is needed to deal with DNA damage and assist in DNA replication during vegetative growth and in meiosis. The interactions of Srs2 with Rad51 Recombinase and proliferating cell nuclear Antigen PCNA are dispensable for the main role of Srs2. | The Main Role of Srs2 in DNA Repair Depends on Its Helicase Activity, Rather than on Its Interactions with PCNA or Rad51.
Bronstein A, Gershon L, Grinberg G, Alonso-Perez E, Kupiec M., Free PMC Article | 07/27/2019 |
| Two main activities of Srs2, strippase and helicase, counteract toxic joint intermediates formed during break-induced replication by preventing their formation and promoting their disruption, respectively. | Break-induced replication promotes formation of lethal joint molecules dissolved by Srs2.
Elango R, Sheng Z, Jackson J, DeCata J, Ibrahim Y, Pham NT, Liang DH, Sakofsky CJ, Vindigni A, Lobachev KS, Ira G, Malkova A., Free PMC Article | 09/22/2018 |
| Srs2 rapidly disrupts small heteroduplex DNA joints bound to Rad51 filaments. | Dissociation of Rad51 Presynaptic Complexes and Heteroduplex DNA Joints by Tandem Assemblies of Srs2.
Kaniecki K, De Tullio L, Gibb B, Kwon Y, Sung P, Greene EC., Free PMC Article | 07/28/2018 |
| These data establish a biochemical mechanism for the role of Srs2 in crossover suppression by promoting synthesis-dependent strand annealing through disruption of DNA polymerase delta-extended D-loops. | Srs2 promotes synthesis-dependent strand annealing by disrupting DNA polymerase δ-extending D-loops.
Liu J, Ede C, Wright WD, Gore SK, Jenkins SS, Freudenthal BD, Todd Washington M, Veaute X, Heyer WD., Free PMC Article | 02/17/2018 |
| Srs2 interaction with PCNA allows the helicase activity to unwind fork-blocking CAG/CTG hairpin structures to prevent DNA breaks during DNA replication. Independently of PCNA binding, Srs2 also displaces Rad51 from nascent strands to prevent recombination-dependent repeat expansions and contractions. | Differential requirement of Srs2 helicase and Rad51 displacement activities in replication of hairpin-forming CAG/CTG repeats.
Nguyen JHG, Viterbo D, Anand RP, Verra L, Sloan L, Richard GF, Freudenreich CH., Free PMC Article | 09/9/2017 |
| Uls1 contributes to the pathway where intermediates generated at replication forks are dismantled by Srs2 bound to SUMO-PCNA. Upon ULS1 deletion, accumulating Srs2-SUMO-unable to bind PCNA-takes part in an alternative PCNA-independent recombination repair salvage pathway(s) | DNA Damage Tolerance Pathway Choice Through Uls1 Modulation of Srs2 SUMOylation in Saccharomyces cerevisiae.
Kramarz K, Mucha S, Litwin I, Barg-Wojas A, Wysocki R, Dziadkowiec D., Free PMC Article | 07/15/2017 |
| Our data suggest that Srs2 and Mus81-Mms4 have critical roles in preventing the formation of (or in resolving) toxic inter-homolog joint molecules, which could otherwise interfere with chromosome segregation and lead to genetic instability. | Srs2 and Mus81-Mms4 Prevent Accumulation of Toxic Inter-Homolog Recombination Intermediates.
Keyamura K, Arai K, Hishida T., Free PMC Article | 03/25/2017 |
| Pro-recombination Role of Srs2 Protein Requires SUMO (Small Ubiquitin-like Modifier) but Is Independent of PCNA (Proliferating Cell Nuclear Antigen) Interaction. | Pro-recombination Role of Srs2 Protein Requires SUMO (Small Ubiquitin-like Modifier) but Is Independent of PCNA (Proliferating Cell Nuclear Antigen) Interaction.
Kolesar P, Altmannova V, Silva S, Lisby M, Krejci L., Free PMC Article | 08/20/2016 |
| Srs2 unfolds trinucleotide repeat hairpin repetitively, and its activity depends on the folding strength and the total length of TNR hairpin. | Molecular mechanism of resolving trinucleotide repeat hairpin by helicases.
Qiu Y, Niu H, Vukovic L, Sung P, Myong S., Free PMC Article | 03/12/2016 |
| Authors discuss the interplay of POL30 and Srs2 proteins in error-free DNA-damage tolerance in Saccharomyces cerevisiae and show how sumoylated PCNA recruits Srs2 for this mechanism. [Review] | Error-free DNA-damage tolerance in Saccharomyces cerevisiae.
Xu X, Blackwell S, Lin A, Li F, Qin Z, Xiao W. | 08/15/2015 |
| data point to a coordinated role of Mus81-Mms4 and Srs2 in processing of recombination as well as replication intermediates | Srs2 promotes Mus81-Mms4-mediated resolution of recombination intermediates.
Chavdarova M, Marini V, Sisakova A, Sedlackova H, Vigasova D, Brill SJ, Lisby M, Krejci L., Free PMC Article | 07/25/2015 |
| When Rad51 is bound on the double-stranded DNA, its interaction with Srs2 blocks the helicase (DNA unwinding) activity of Srs2. | Context-dependent remodeling of Rad51-DNA complexes by Srs2 is mediated by a specific protein-protein interaction.
Lytle AK, Origanti SS, Qiu Y, VonGermeten J, Myong S, Antony E. | 06/14/2014 |
| Srs2 exhibits ATP-dependent repetitive motion on single-stranded DNA and this activity prevents re-formation of the Rad51 filament. | Srs2 prevents Rad51 filament formation by repetitive motion on DNA.
Qiu Y, Antony E, Doganay S, Koh HR, Lohman TM, Myong S., Free PMC Article | 04/12/2014 |
| Rad52 mutant cannot restore viability of srs2Delta cells that accumulate intertwined recombination intermediates which are normally processed by Srs2 post-synaptic functions | Rad52 sumoylation prevents the toxicity of unproductive Rad51 filaments independently of the anti-recombinase Srs2.
Esta A, Ma E, Dupaigne P, Maloisel L, Guerois R, Le Cam E, Veaute X, Coïc E., Free PMC Article | 03/22/2014 |
| Srs2 disrupts Rad51-containing complexes from chromosomes during meiosis. | Remodeling of the Rad51 DNA strand-exchange protein by the Srs2 helicase.
Sasanuma H, Furihata Y, Shinohara M, Shinohara A., Free PMC Article | 02/22/2014 |
| Putative antirecombinase Srs2 DNA helicase promotes noncrossover homologous recombination avoiding loss of heterozygosity. | Putative antirecombinase Srs2 DNA helicase promotes noncrossover homologous recombination avoiding loss of heterozygosity.
Miura T, Shibata T, Kusano K., Free PMC Article | 12/7/2013 |
| The hDNA data are consistent with the proposed role of Sgs1 in the dissolution of double HJs, and we propose that Srs2 dismantles nicked HJs. | Heteroduplex DNA position defines the roles of the Sgs1, Srs2, and Mph1 helicases in promoting distinct recombination outcomes.
Mitchel K, Lehner K, Jinks-Robertson S., Free PMC Article | 06/15/2013 |
| Srs2 unwinding is inhibited by ssDNA binding protein RPA in vitro | Unwinding of synthetic replication and recombination substrates by Srs2.
Marini V, Krejci L., Free PMC Article | 01/26/2013 |
| The SUMO-interacting motif region is required for Srs2 sumoylation, likely by binding to SUMO-charged Ubc9. | Dual roles of the SUMO-interacting motif in the regulation of Srs2 sumoylation.
Kolesar P, Sarangi P, Altmannova V, Zhao X, Krejci L., Free PMC Article | 11/24/2012 |
| suppression of homologous recombination in postreplication repair-deficient cells by Srs2 and PCNA sumoylation is required for checkpoint activation and checkpoint maintenance during UV irradiation | Srs2 plays a critical role in reversible G2 arrest upon chronic and low doses of UV irradiation via two distinct homologous recombination-dependent mechanisms in postreplication repair-deficient cells.
Hishida T, Hirade Y, Haruta N, Kubota Y, Iwasaki H., Free PMC Article | 10/30/2010 |