| The cruciform DNA-binding protein Crp1 stimulates the endonuclease activity of Mus81-Mms4 in Saccharomyces cerevisiae. | The cruciform DNA-binding protein Crp1 stimulates the endonuclease activity of Mus81-Mms4 in Saccharomyces cerevisiae.
Phung HTT, Tran DH, Nguyen TX. | 06/5/2021 |
| Mus81-Mms4 endonuclease is an Esc2-STUbL-Cullin8 mitotic substrate impacting on genome integrity. | Mus81-Mms4 endonuclease is an Esc2-STUbL-Cullin8 mitotic substrate impacting on genome integrity.
Waizenegger A, Urulangodi M, Lehmann CP, Reyes TAC, Saugar I, Tercero JA, Szakal B, Branzei D., Free PMC Article | 12/5/2020 |
| Study presents evidence that yeast Mus81-Mms4 endonuclease contributes to cell viability in the absence of functional telomerase. This involvement is not through recombination-mediated telomere lengthening as proposed in humans, but rather through an indirect role involving replication stress. | Saccharomyces cerevisiae Mus81-Mms4 prevents accelerated senescence in telomerase-deficient cells.
Schwartz EK, Hung SH, Meyer D, Piazza A, Yan K, Fu BXH, Heyer WD., Free PMC Article | 08/1/2020 |
| These results strongly support the notion that Rad52 and Mus81-Mms4 collaborate and work jointly in processing of homologous recombination intermediates. | Saccharomyces cerevisiae Mus81-Mms4 and Rad52 can cooperate in the resolution of recombination intermediates.
Phung HTT, Nguyen HLH, Vo ST, Nguyen DH, Le MV. | 03/2/2019 |
| Identification of new interacting partners and modulators of Mus81-Mms4 nuclease, RFC, and PCNA imply the cooperation of these factors in resolution of stalled replication forks and branched DNA structures emanating from the restarted replication forks under conditions of replication stress. | Role of PCNA and RFC in promoting Mus81-complex activity.
Sisakova A, Altmannova V, Sebesta M, Krejci L., Free PMC Article | 05/19/2018 |
| The scaffold protein Rtt107, which binds the Mus81-Mms4 complex, interacts with Cdc7 and thereby targets Cdc7-Dbf4 and Cdc5 to the complex enabling full Mus81 activation. | Dbf4-dependent kinase and the Rtt107 scaffold promote Mus81-Mms4 resolvase activation during mitosis.
Princz LN, Wild P, Bittmann J, Aguado FJ, Blanco MG, Matos J, Pfander B., Free PMC Article | 07/8/2017 |
| 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 |
| The role of Mms4 in crossover formation during meiotic recombinational repair | Controlling meiotic recombinational repair - specifying the roles of ZMMs, Sgs1 and Mus81/Mms4 in crossover formation.
Oke A, Anderson CM, Yam P, Fung JC., Free PMC Article | 04/30/2016 |
| Unresolved recombination intermediates are a source of mitotic sister chromatid bridges, and Mus81-Mms4 and Yen1 play a central role in their resolution in vivo. | Mus81-Mms4 and Yen1 resolve a novel anaphase bridge formed by noncanonical Holliday junctions.
García-Luis J, Machín F. | 10/31/2015 |
| 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 |
| The data indicates that Mus81-Mms4 activation is not induced by the presence of DNA lesions and that its function to respond to DNA damage, which allows cell survival, is carried out after completion of bulk genome replication. | Temporal regulation of the Mus81-Mms4 endonuclease ensures cell survival under conditions of DNA damage.
Saugar I, Vázquez MV, Gallo-Fernández M, Ortiz-Bazán MÁ, Segurado M, Calzada A, Tercero JA., Free PMC Article | 01/4/2014 |
| Suggest that Mph1 and Mus81-Mms4 recognize an early strand exchange intermediate and direct repair to noncrossover or crossover outcomes, respectively. | Mph1 and Mus81-Mms4 prevent aberrant processing of mitotic recombination intermediates.
Mazón G, Symington LS., Free PMC Article | 12/7/2013 |
| data support a model in which Mus81-Mms4 cleaves nicked recombination intermediates such as displacement loops (D-loops), nicked Holliday junctions, or 3' flaps but not intact Holliday junctions with four uninterrupted strands | Mus81-Mms4 functions as a single heterodimer to cleave nicked intermediates in recombinational DNA repair.
Schwartz EK, Wright WD, Ehmsen KT, Evans JE, Stahlberg H, Heyer WD., Free PMC Article | 10/13/2012 |
| Functional overlap between the structure-specific nucleases Yen1 and Mus81-Mms4 for DNA-damage repair in S. cerevisiae | Functional overlap between the structure-specific nucleases Yen1 and Mus81-Mms4 for DNA-damage repair in S. cerevisiae.
Blanco MG, Matos J, Rass U, Ip SC, West SC. | 07/5/2010 |
| Results indicate that Mus81-Mms4, unlike FEN1/Rad27, does not prefer dually flapped substrates and is unlikely to function as a 3'-flapase counterpart to the 5'-flapase activity of FEN1/Rad27. | A junction branch point adjacent to a DNA backbone nick directs substrate cleavage by Saccharomyces cerevisiae Mus81-Mms4.
Ehmsen KT, Heyer WD., Free PMC Article | 01/21/2010 |
| Sgs1 and Mus81-Mms4 collaborate to eliminate aberrant JMs, whereas as-yet-unidentified enzymes process normal joint molecules. | RecQ helicase, Sgs1, and XPF family endonuclease, Mus81-Mms4, resolve aberrant joint molecules during meiotic recombination.
Oh SD, Lao JP, Taylor AF, Smith GR, Hunter N., Free PMC Article | 01/21/2010 |
| These results indicate that Sgs1 and Mus81/Mms4 collaborate to direct meiotic recombination toward interhomolog interactions that promote proper chromosome segregation, and also indicate that Mus81/Mms4 promotes joint molecules resolution in vivo. | Mus81/Mms4 endonuclease and Sgs1 helicase collaborate to ensure proper recombination intermediate metabolism during meiosis.
Jessop L, Lichten M., Free PMC Article | 01/21/2010 |
| A kinetic analysis of Mus81-Mms4 cleavage, and a quantitative comparison of its substrate selectivity. | Saccharomyces cerevisiae Mus81-Mms4 is a catalytic, DNA structure-selective endonuclease.
Ehmsen KT, Heyer WD., Free PMC Article | 01/21/2010 |