메뉴 건너뛰기




Volumn 45, Issue 1, 2017, Pages 215-230

Esc2 promotes Mus81 complex-activity via its SUMO-like and DNA binding domains

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; ENDONUCLEASE; ESTABLISHMENT OF SILENT CHROMATIN 2; MUS81 COMPLEX; SUMO PROTEIN; UNCLASSIFIED DRUG; CRUCIFORM DNA; DNA BINDING PROTEIN; ESC2 PROTEIN, S CEREVISIAE; FUNGAL DNA; MUS81 PROTEIN, S CEREVISIAE; NUCLEAR PROTEIN; PROTEIN BINDING; RECOMBINANT PROTEIN; SACCHAROMYCES CEREVISIAE PROTEIN;

EID: 85015979687     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkw882     Document Type: Article
Times cited : (21)

References (72)
  • 1
    • 70350504453 scopus 로고    scopus 로고
    • The DNA-damage response in human biology and disease
    • Jackson, S. P. and Bartek, J. (2009) The DNA-damage response in human biology and disease. Nature, 461, 1071-1078.
    • (2009) Nature , vol.461 , pp. 1071-1078
    • Jackson, S.P.1    Bartek, J.2
  • 2
    • 80052768689 scopus 로고    scopus 로고
    • Ubiquitin family modifications and template switching
    • Branzei, D. (2011) Ubiquitin family modifications and template switching. FEBS Lett., 585, 2810-2817.
    • (2011) FEBS Lett. , vol.585 , pp. 2810-2817
    • Branzei, D.1
  • 3
    • 80052702417 scopus 로고    scopus 로고
    • Timing and spacing of ubiquitin-dependent DNA damage bypass
    • Ulrich, H. D. (2011) Timing and spacing of ubiquitin-dependent DNA damage bypass. FEBS Lett., 585, 2861-2867.
    • (2011) FEBS Lett. , vol.585 , pp. 2861-2867
    • Ulrich, H.D.1
  • 4
    • 27644590452 scopus 로고    scopus 로고
    • The error-free component of the RAD6/RAD18 DNA damage tolerance pathway of budding yeast employs sister-strand recombination
    • Zhang, H. and Lawrence, C. W. (2005) The error-free component of the RAD6/RAD18 DNA damage tolerance pathway of budding yeast employs sister-strand recombination. Proc. Natl. Acad. Sci. U. S. A., 102, 15954-15959.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 15954-15959
    • Zhang, H.1    Lawrence, C.W.2
  • 5
    • 57749169348 scopus 로고    scopus 로고
    • SUMOylation regulates Rad18-mediated template switch
    • Branzei, D., Vanoli, F. and Foiani, M. (2008) SUMOylation regulates Rad18-mediated template switch. Nature, 456, 915-920.
    • (2008) Nature , vol.456 , pp. 915-920
    • Branzei, D.1    Vanoli, F.2    Foiani, M.3
  • 6
    • 77953085206 scopus 로고    scopus 로고
    • Multiple Rad5 activities mediate sister chromatid recombination to bypass DNA damage at stalled replication forks
    • Minca, E. C. and Kowalski, D. (2010) Multiple Rad5 activities mediate sister chromatid recombination to bypass DNA damage at stalled replication forks. Mol. Cell, 38, 649-661.
    • (2010) Mol. Cell , vol.38 , pp. 649-661
    • Minca, E.C.1    Kowalski, D.2
  • 7
    • 78649702212 scopus 로고    scopus 로고
    • Replication and recombination factors contributing to recombination-dependent bypass of DNA lesions by template switch
    • Vanoli, F., Fumasoni, M., Szakal, B., Maloisel, L. and Branzei, D. (2010) Replication and recombination factors contributing to recombination-dependent bypass of DNA lesions by template switch. PLoS Genet., 6, e1001205.
    • (2010) PLoS Genet. , vol.6 , pp. e1001205
    • Vanoli, F.1    Fumasoni, M.2    Szakal, B.3    Maloisel, L.4    Branzei, D.5
  • 8
    • 84873425410 scopus 로고    scopus 로고
    • Noncanonical role of the 9-1-1 clamp in the error-free DNA damage tolerance pathway
    • Karras, G. I., Fumasoni, M., Sienski, G., Vanoli, F., Branzei, D. and Jentsch, S. (2012) Noncanonical role of the 9-1-1 clamp in the error-free DNA damage tolerance pathway. Mol. Cell, doi:10.1016/j.molcel.2012.11.016.
    • (2012) Mol. Cell
    • Karras, G.I.1    Fumasoni, M.2    Sienski, G.3    Vanoli, F.4    Branzei, D.5    Jentsch, S.6
  • 9
    • 84876407519 scopus 로고    scopus 로고
    • Premature Cdk1/Cdc5/Mus81 pathway activation induces aberrant replication and deleterious crossover
    • Szakal, B. and Branzei, D. (2013) Premature Cdk1/Cdc5/Mus81 pathway activation induces aberrant replication and deleterious crossover. EMBO J., 32, 1155-1167.
    • (2013) EMBO J. , vol.32 , pp. 1155-1167
    • Szakal, B.1    Branzei, D.2
  • 10
    • 79955456518 scopus 로고    scopus 로고
    • Pathways for Holliday junction processing during homologous recombination in Saccharomyces cerevisiae
    • Ashton, T. M., Mankouri, H. W., Heidenblut, A., McHugh, P. J. and Hickson, I. D. (2011) Pathways for Holliday junction processing during homologous recombination in Saccharomyces cerevisiae. Mol. Cell. Biol., 31, 1921-1933.
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 1921-1933
    • Ashton, T.M.1    Mankouri, H.W.2    Heidenblut, A.3    McHugh, P.J.4    Hickson, I.D.5
  • 11
    • 0043092025 scopus 로고    scopus 로고
    • Identification and characterization of the human Mus81-Eme1 endonuclease
    • Ciccia, A., Constantinou, A. and West, SC. (2003) Identification and characterization of the human Mus81-Eme1 endonuclease. J. Biol. Chem., 278, 25172-25178.
    • (2003) J. Biol. Chem. , vol.278 , pp. 25172-25178
    • Ciccia, A.1    Constantinou, A.2    West, S.C.3
  • 12
    • 0037470059 scopus 로고    scopus 로고
    • Cleavage of model replication forks by fssion yeast Mus81-Eme1 and budding yeast Mus81-Mms4
    • Whitby, M. C., Osman, F. and Dixon, J. (2003) Cleavage of model replication forks by fssion yeast Mus81-Eme1 and budding yeast Mus81-Mms4. J. Biol. Chem., 278, 6928-6935.
    • (2003) J. Biol. Chem. , vol.278 , pp. 6928-6935
    • Whitby, M.C.1    Osman, F.2    Dixon, J.3
  • 13
    • 0038498093 scopus 로고    scopus 로고
    • Identification and characterization of human MUS81-MMS4 structure-specific endonuclease
    • Ogrunc, M. and Sancar, A. (2003) Identification and characterization of human MUS81-MMS4 structure-specific endonuclease. J. Biol. Chem., 278, 21715-21720.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21715-21720
    • Ogrunc, M.1    Sancar, A.2
  • 14
    • 10044292849 scopus 로고    scopus 로고
    • Substrate specificity of the Saccharomyces cerevisiae Mus81-Mms4 endonuclease
    • Fricke, W. M., Bastin-Shanower, S. A. and Brill, S. J. (2005) Substrate specificity of the Saccharomyces cerevisiae Mus81-Mms4 endonuclease. DNA Repair (Amst.), 4, 243-251.
    • (2005) DNA Repair (Amst.) , vol.4 , pp. 243-251
    • Fricke, W.M.1    Bastin-Shanower, S.A.2    Brill, S.J.3
  • 15
    • 42449115326 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Mus81-Mms4 is a catalytic, DNA structure-selective endonuclease
    • Ehmsen, K. T. and Heyer, W. D. (2008) Saccharomyces cerevisiae Mus81-Mms4 is a catalytic, DNA structure-selective endonuclease. Nucleic Acids Res., 36, 2182-2195.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 2182-2195
    • Ehmsen, K.T.1    Heyer, W.D.2
  • 16
    • 0033830809 scopus 로고    scopus 로고
    • MUS81 encodes a novel Helix-hairpin-Helix protein involved in the response to UV- and methylation-induced DNA damage in Saccharomyces cerevisiae
    • Interthal, H. and Heyer, W. D. (2000) MUS81 encodes a novel Helix-hairpin-Helix protein involved in the response to UV- and methylation-induced DNA damage in Saccharomyces cerevisiae. Mol. Gen. Genet. MGG, 263, 812-827.
    • (2000) Mol. Gen. Genet. MGG , vol.263 , pp. 812-827
    • Interthal, H.1    Heyer, W.D.2
  • 17
    • 34249942213 scopus 로고    scopus 로고
    • Exploring the roles of Mus81-Eme1/Mms4 at perturbed replication forks
    • Osman, F. and Whitby, M. (2007) Exploring the roles of Mus81-Eme1/Mms4 at perturbed replication forks. DNA Repair (Amst.), 6, 1004-1017.
    • (2007) DNA Repair (Amst.) , vol.6 , pp. 1004-1017
    • Osman, F.1    Whitby, M.2
  • 18
  • 20
    • 34447536139 scopus 로고    scopus 로고
    • BLM ortholog, Sgs1, prevents aberrant crossing-over by suppressing formation of multichromatid joint molecules
    • Oh, S. D., Lao, J. P., Hwang, P. Y.-H., Taylor, A. F., Smith, G. R. and Hunter, N. (2008) BLM ortholog, Sgs1, prevents aberrant crossing-over by suppressing formation of multichromatid joint molecules. Cell, 130, 259-272.
    • (2008) Cell , vol.130 , pp. 259-272
    • Oh, S.D.1    Lao, J.P.2    Hwang, P.Y.-H.3    Taylor, A.F.4    Smith, G.R.5    Hunter, N.6
  • 21
    • 48349141924 scopus 로고    scopus 로고
    • Mus81/Mms4 endonuclease and Sgs1 helicase collaborate to ensure proper recombination intermediate metabolism during meiosis
    • Jessop, L. and Lichten, M. (2008) Mus81/Mms4 endonuclease and Sgs1 helicase collaborate to ensure proper recombination intermediate metabolism during meiosis. Mol. Cell, 31, 313-323.
    • (2008) Mol. Cell , vol.31 , pp. 313-323
    • Jessop, L.1    Lichten, M.2
  • 23
    • 84881471113 scopus 로고    scopus 로고
    • ERCC1 and MUS81-EME1 promote sister chromatid separation by processing late replication intermediates at common fragile sites during mitosis
    • Naim, V., Wilhelm, T., Debatisse, M. and Rosselli, F. (2013) ERCC1 and MUS81-EME1 promote sister chromatid separation by processing late replication intermediates at common fragile sites during mitosis. Nat. Cell Biol., 15, 1008-1015.
    • (2013) Nat. Cell Biol. , vol.15 , pp. 1008-1015
    • Naim, V.1    Wilhelm, T.2    Debatisse, M.3    Rosselli, F.4
  • 25
    • 80053544629 scopus 로고    scopus 로고
    • Regulatory control of the resolution of DNA recombination intermediates during meiosis and mitosis
    • Matos, J., Blanco, M. G., Maslen, S., Skehel, J. M. and West, S. C. (2011) Regulatory control of the resolution of DNA recombination intermediates during meiosis and mitosis. Cell, 147, 158-172.
    • (2011) Cell , vol.147 , pp. 158-172
    • Matos, J.1    Blanco, M.G.2    Maslen, S.3    Skehel, J.M.4    West, S.C.5
  • 28
    • 0033638234 scopus 로고    scopus 로고
    • A histone variant, Htz1p, and a Sir1p-like protein, Esc2p, mediate silencing at HMR
    • Dhillon, N. and Kamakaka, R. T. (2000) A Histone Variant, Htz1p, and a Sir1p-like Protein, Esc2p, Mediate Silencing at HMR. Mol. Cell, 6, 769-780.
    • (2000) Mol. Cell , vol.6 , pp. 769-780
    • Dhillon, N.1    Kamakaka, R.T.2
  • 29
    • 25444484394 scopus 로고    scopus 로고
    • Proteins with two SUMO/like domains in chromatin/associated complexes: The RENi (Rad60/Esc2/NIP45) family
    • Novatchkova, M., Bachmair, A., Eisenhaber, B. and Eisenhaber, F. (2005) Proteins with two SUMO/like domains in chromatin/associated complexes: The RENi (Rad60/Esc2/NIP45) family. BMC Bioinformatics, 6, 22.
    • (2005) BMC Bioinformatics , vol.6 , pp. 22
    • Novatchkova, M.1    Bachmair, A.2    Eisenhaber, B.3    Eisenhaber, F.4
  • 30
    • 65249118311 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae Esc2 and Smc5-6 Proteins Promote Sister Chromatid Junction-mediated Intra-S Repair
    • Sollier, J., Driscoll, R., Castellucci, F., Foiani, M., Jackson, S. P. and Branzei, D. (2009) The Saccharomyces cerevisiae Esc2 and Smc5-6 Proteins Promote Sister Chromatid Junction-mediated Intra-S Repair. Mol. Biol. Cell, 20, 1671-1682.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1671-1682
    • Sollier, J.1    Driscoll, R.2    Castellucci, F.3    Foiani, M.4    Jackson, S.P.5    Branzei, D.6
  • 31
    • 65249090885 scopus 로고    scopus 로고
    • Esc2 and Sgs1 act in functionally distinct branches of the homologous recombination repair pathway in Saccharomyces cerevisiae
    • Mankouri, H. W., Ngo, H.-P. and Hickson, I. D. (2009) Esc2 and Sgs1 act in functionally distinct branches of the homologous recombination repair pathway in Saccharomyces cerevisiae. Mol. Biol. Cell, 20, 1683-1694.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1683-1694
    • Mankouri, H.W.1    Ngo, H.-P.2    Hickson, I.D.3
  • 32
    • 84943531043 scopus 로고    scopus 로고
    • Local regulation of the Srs2 helicase by the SUMO-like domain protein Esc2 promotes recombination at sites of stalled replication
    • Urulangodi, M., Sebesta, M., Menolf, D., Szakal, B., Sollier, J., Sisakova, A., Krejci, L. and Branzei, D. (2015) Local regulation of the Srs2 helicase by the SUMO-like domain protein Esc2 promotes recombination at sites of stalled replication. Genes Dev., 29, 2067-2080.
    • (2015) Genes Dev. , vol.29 , pp. 2067-2080
    • Urulangodi, M.1    Sebesta, M.2    Menolf, D.3    Szakal, B.4    Sollier, J.5    Sisakova, A.6    Krejci, L.7    Branzei, D.8
  • 33
    • 0024977417 scopus 로고
    • Elevated recombination rates in transcriptionally active DNA
    • Thomas, B. J. and Rothstein, R. (1989) Elevated recombination rates in transcriptionally active DNA. Cell, 56, 619-630.
    • (1989) Cell , vol.56 , pp. 619-630
    • Thomas, B.J.1    Rothstein, R.2
  • 34
    • 65549118806 scopus 로고    scopus 로고
    • Cooperativity of Mus81·Mms4 with Rad54 in the resolution of recombination and replication intermediates
    • Matulova, P., Marini, V., Burgess, R. C., Sisakova, A., Kwon, Y., Rothstein, R., Sung, P. and Krejci, L. (2009) Cooperativity of Mus81·Mms4 with Rad54 in the resolution of recombination and replication intermediates. J. Biol. Chem., 284, 7733-7745.
    • (2009) J. Biol. Chem. , vol.284 , pp. 7733-7745
    • Matulova, P.1    Marini, V.2    Burgess, R.C.3    Sisakova, A.4    Kwon, Y.5    Rothstein, R.6    Sung, P.7    Krejci, L.8
  • 35
    • 84868575414 scopus 로고    scopus 로고
    • Live cell microscopy of DNA damage response in Saccharomyces cerevisiae
    • Silva, S., Gallina, I., Eckert-Boulet, N. and Lisby, M. (2012) Live cell microscopy of DNA damage response in Saccharomyces cerevisiae. Methods Mol Biol., 920, 433-443.
    • (2012) Methods Mol Biol. , vol.920 , pp. 433-443
    • Silva, S.1    Gallina, I.2    Eckert-Boulet, N.3    Lisby, M.4
  • 36
    • 0029847806 scopus 로고    scopus 로고
    • Crystal structure of the Aequorea Victoria green fluorescent protein
    • Orm, M., Cubitt, A. B., Kallio, K., Gross, L. A., Tsien, R. Y. and Remington, S. J. (1996) Crystal structure of the Aequorea victoria green fluorescent protein. Science, 273, 1392-1395.
    • (1996) Science , vol.273 , pp. 1392-1395
    • Orm, M.1    Cubitt, A.B.2    Kallio, K.3    Gross, L.A.4    Tsien, R.Y.5    Remington, S.J.6
  • 38
    • 84904254378 scopus 로고    scopus 로고
    • Nucleases in homologous recombination as targets for cancer therapy
    • Bartosova, Z. and Krejci, L. (2014) Nucleases in homologous recombination as targets for cancer therapy. FEBS Lett., 588, 2446-2456.
    • (2014) FEBS Lett. , vol.588 , pp. 2446-2456
    • Bartosova, Z.1    Krejci, L.2
  • 39
    • 0037449738 scopus 로고    scopus 로고
    • Okazaki fragment maturation in yeast: I. Distribution of functions between FEN1 and DNA2
    • Ayyagari, R., Gomes, X. V., Gordenin, D. A. and Burgers, P. M. J. (2003) Okazaki fragment maturation in yeast: I. Distribution of functions between FEN1 and DNA2. J. Biol. Chem., 278, 1618-1625.
    • (2003) J. Biol. Chem. , vol.278 , pp. 1618-1625
    • Ayyagari, R.1    Gomes, X.V.2    Gordenin, D.A.3    Burgers, P.M.J.4
  • 40
    • 0037177823 scopus 로고    scopus 로고
    • Cleavage specificity of Saccharomyces cerevisiae fap endonuclease 1 suggests a double-fap structure as the cellular substrate
    • Kao, H. I., Henricksen, L. A., Liu, Y. and Bambara, R. A. (2002) Cleavage specificity of Saccharomyces cerevisiae fap endonuclease 1 suggests a double-fap structure as the cellular substrate. J. Biol. Chem., 277, 14379-14389.
    • (2002) J. Biol. Chem. , vol.277 , pp. 14379-14389
    • Kao, H.I.1    Henricksen, L.A.2    Liu, Y.3    Bambara, R.A.4
  • 41
    • 0027225340 scopus 로고
    • Yeast DNA repair and recombination proteins Rad1 and Rad10 constitute a single-stranded-DNA endonuclease
    • Tomkinson, A. E., Bardwell, A. J., Bardwell, L., Tappe, N. J. and Friedberg, E. C. (1993) Yeast DNA repair and recombination proteins Rad1 and Rad10 constitute a single-stranded-DNA endonuclease. Nature, 362, 860-862.
    • (1993) Nature , vol.362 , pp. 860-862
    • Tomkinson, A.E.1    Bardwell, A.J.2    Bardwell, L.3    Tappe, N.J.4    Friedberg, E.C.5
  • 44
    • 56749119855 scopus 로고    scopus 로고
    • Identification of Holliday junction resolvases from humans and yeast
    • Ip, S. C. Y., Rass, U., Blanco, M. G., Flynn, H. R., Skehel, J. M. and West, S. C. (2008) Identification of Holliday junction resolvases from humans and yeast. Nature, 456, 357-361.
    • (2008) Nature , vol.456 , pp. 357-361
    • Ip, S.C.Y.1    Rass, U.2    Blanco, M.G.3    Flynn, H.R.4    Skehel, J.M.5    West, S.C.6
  • 45
    • 78650242581 scopus 로고    scopus 로고
    • Mus81 and Yen1 promote reciprocal exchange during mitotic recombination to maintain genome integrity in budding yeast
    • Ho, C. K., Mazón, G., Lam, A. F. and Symington, L. S. (2010) Mus81 and Yen1 promote reciprocal exchange during mitotic recombination to maintain genome integrity in budding yeast. Mol. Cell, 40, 988-1000.
    • (2010) Mol. Cell , vol.40 , pp. 988-1000
    • Ho, C.K.1    Mazón, G.2    Lam, A.F.3    Symington, L.S.4
  • 46
    • 77949653925 scopus 로고    scopus 로고
    • Functional overlap between the structure-specific nucleases Yen1 and Mus81-Mms4 for DNA-damage repair in S
    • Blanco, M. G., Matos, J., Rass, U., Ip, S. C. Y. and West, S. C. (2010) Functional overlap between the structure-specific nucleases Yen1 and Mus81-Mms4 for DNA-damage repair in S. cerevisiae. DNA Repair (Amst.), 9, 394-402.
    • (2010) Cerevisiae. DNA Repair (Amst.) , vol.9 , pp. 394-402
    • Blanco, M.G.1    Matos, J.2    Rass, U.3    Ip, S.C.Y.4    West, S.C.5
  • 48
    • 0034119866 scopus 로고    scopus 로고
    • Homologous recombination is responsible for cell death in the absence of the Sgs1 and Srs2 helicases
    • Gangloff, S., Fabre, F. and Soustelle, C. (2000) Homologous recombination is responsible for cell death in the absence of the Sgs1 and Srs2 helicases. Nat. Genet., 25, 192-194.
    • (2000) Nat. Genet. , vol.25 , pp. 192-194
    • Gangloff, S.1    Fabre, F.2    Soustelle, C.3
  • 50
    • 77649165394 scopus 로고    scopus 로고
    • Maintaining genome stability at the replication fork
    • Branzei, D. and Foiani, M. (2010) Maintaining genome stability at the replication fork. Nat Rev Mol Cell Biol., 11, 208-219.
    • (2010) Nat Rev Mol Cell Biol. , vol.11 , pp. 208-219
    • Branzei, D.1    Foiani, M.2
  • 51
    • 1842427563 scopus 로고    scopus 로고
    • The extended left-handed helix: A simple nucleic acid-binding motif
    • Hicks, J. M. and Hsu, V. L. (2004) The extended left-handed helix: a simple nucleic acid-binding motif. Proteins, 55, 330-338.
    • (2004) Proteins , vol.55 , pp. 330-338
    • Hicks, J.M.1    Hsu, V.L.2
  • 52
    • 0029058133 scopus 로고
    • The importance of extended conformations and, in particular, the PII conformation for the molecular recognition of peptides
    • Siligardi, G. and Drake, A. F. (1995) The importance of extended conformations and, in particular, the PII conformation for the molecular recognition of peptides. Biopolymers, 37, 281-292.
    • (1995) Biopolymers , vol.37 , pp. 281-292
    • Siligardi, G.1    Drake, A.F.2
  • 53
    • 35348986443 scopus 로고    scopus 로고
    • Binding and activation of DNA topoisomerase III by the Rmi1 subunit
    • Chen, C.-F. and Brill, S. J. (2007) Binding and activation of DNA topoisomerase III by the Rmi1 subunit. J. Biol. Chem., 282, 28971-28979.
    • (2007) J. Biol. Chem. , vol.282 , pp. 28971-28979
    • Chen, C.-F.1    Brill, S.J.2
  • 54
  • 55
  • 56
    • 28844455305 scopus 로고    scopus 로고
    • Small ubiquitin-like modifier (SUMO) recognition of a SUMO binding motif: A reversal of the bound orientation
    • Song, J., Zhang, Z., Hu, W. and Chen, Y. (2005) Small ubiquitin-like modifier (SUMO) recognition of a SUMO binding motif: a reversal of the bound orientation. J. Biol. Chem., 280, 40122-40129.
    • (2005) J. Biol. Chem. , vol.280 , pp. 40122-40129
    • Song, J.1    Zhang, Z.2    Hu, W.3    Chen, Y.4
  • 57
    • 84869091913 scopus 로고    scopus 로고
    • Protein group modification and synergy in the SUMO pathway as exemplified in DNA repair
    • Psakhye, I. and Jentsch, S. Protein group modification and synergy in the SUMO pathway as exemplified in DNA repair. Cell, 151, 807-820.
    • Cell , vol.151 , pp. 807-820
    • Psakhye, I.1    Jentsch, S.2
  • 58
    • 84888617317 scopus 로고    scopus 로고
    • Control of nuclear activities by substrate-selective and protein-group SUMOylation
    • Jentsch, S. and Psakhye, I. (2013) Control of nuclear activities by substrate-selective and protein-group SUMOylation. Annu. Rev. Genet., 47, 167-186.
    • (2013) Annu. Rev. Genet. , vol.47 , pp. 167-186
    • Jentsch, S.1    Psakhye, I.2
  • 59
    • 84964844250 scopus 로고    scopus 로고
    • Pro-recombination role of Srs2 protein requires SUMO (small ubiquitin-like modifi er) but Is independent of PCNA (proliferating cell nuclear antigen) interaction
    • Kolesar, P., Altmannova, V., Silva, S., Lisby, M. and Krejci, L. (2016) Pro-recombination role of Srs2 protein requires SUMO (small ubiquitin-like modifi er) but Is independent of PCNA (proliferating cell nuclear antigen) interaction. J. Biol. Chem., 291, 7594-7607.
    • (2016) J. Biol. Chem. , vol.291 , pp. 7594-7607
    • Kolesar, P.1    Altmannova, V.2    Silva, S.3    Lisby, M.4    Krejci, L.5
  • 61
    • 0034679597 scopus 로고    scopus 로고
    • Two modes of FEN1 binding to PCNA regulated by DNA
    • Gomes, X. V. and Burgers, P. M. J. (2000) Two modes of FEN1 binding to PCNA regulated by DNA. EMBO J., 19, 3811-3821.
    • (2000) EMBO J. , vol.19 , pp. 3811-3821
    • Gomes, X.V.1    Burgers, P.M.J.2
  • 62
    • 0034616199 scopus 로고    scopus 로고
    • Mechanism whereby proliferating cell nuclear antigen stimulates fap endonuclease 1
    • Tom, S., Henricksen, L. A. and Bambara, R. A. (2000) Mechanism whereby proliferating cell nuclear antigen stimulates fap endonuclease 1. J. Biol. Chem., 275, 10498-10505.
    • (2000) J. Biol. Chem. , vol.275 , pp. 10498-10505
    • Tom, S.1    Henricksen, L.A.2    Bambara, R.A.3
  • 64
    • 57449090470 scopus 로고    scopus 로고
    • Human Rad54 protein stimulates human Mus81-Eme1 endonuclease
    • Mazina, O. M. and Mazin, A. V. (2008) Human Rad54 protein stimulates human Mus81-Eme1 endonuclease. Proc. Natl. Acad. Sci. U. S. A., 105, 18249-18254.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 18249-18254
    • Mazina, O.M.1    Mazin, A.V.2
  • 66
    • 0347987856 scopus 로고    scopus 로고
    • The Bloom's syndrome helicase suppresses crossing over during homologous recombination
    • Wu, L. and Hickson, I. D. (2003) The Bloom's syndrome helicase suppresses crossing over during homologous recombination. Nat. Cell Biol., 426, 870-874.
    • (2003) Nat. Cell Biol. , vol.426 , pp. 870-874
    • Wu, L.1    Hickson, I.D.2
  • 67
    • 84866856051 scopus 로고    scopus 로고
    • Decatenation of DNA by the S. Cerevisiae Sgs1-Top3-Rmi1 and RPA complex: A mechanism for disentangling chromosomes
    • Cejka, P., Plank, J. L., Dombrowski, C. C. and Kowalczykowski, S. C. (2012) Decatenation of DNA by the S. cerevisiae Sgs1-Top3-Rmi1 and RPA complex: a mechanism for disentangling chromosomes. Mol. Cell, 47, 886-896.
    • (2012) Mol. Cell , vol.47 , pp. 886-896
    • Cejka, P.1    Plank, J.L.2    Dombrowski, C.C.3    Kowalczykowski, S.C.4
  • 68
    • 0038167328 scopus 로고    scopus 로고
    • Slx1-Slx4 is a second structure-specific endonuclease functionally redundant with Sgs1-Top3
    • Fricke, W. M. and Brill, S. J. (2003) Slx1-Slx4 is a second structure-specific endonuclease functionally redundant with Sgs1-Top3. Genes Dev., 17, 1768-1778.
    • (2003) Genes Dev. , vol.17 , pp. 1768-1778
    • Fricke, W.M.1    Brill, S.J.2
  • 69
    • 84859714621 scopus 로고    scopus 로고
    • Delineation of joint molecule resolution pathways in meiosis identifies a crossover-specific resolvase
    • Zakharyevich, K., Tang, S., Ma, Y. and Hunter, N. (2012) Delineation of joint molecule resolution pathways in meiosis identifies a crossover-specific resolvase. Cell, 149, 334-347.
    • (2012) Cell , vol.149 , pp. 334-347
    • Zakharyevich, K.1    Tang, S.2    Ma, Y.3    Hunter, N.4
  • 70
    • 84896874313 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae Mlh1-Mlh3 heterodimer Is an endonuclease that preferentially binds to Holliday junctions
    • Ranjha, L., Anand, R. and Cejka, P. (2014) The Saccharomyces cerevisiae Mlh1-Mlh3 heterodimer Is an endonuclease that preferentially binds to Holliday junctions. J. Biol. Chem., 289, 5674-5686.
    • (2014) J. Biol. Chem. , vol.289 , pp. 5674-5686
    • Ranjha, L.1    Anand, R.2    Cejka, P.3
  • 71
    • 0041966011 scopus 로고    scopus 로고
    • Elg1 forms an alternative RFIC complex important for DNA replication and genome integrity
    • Bellaoui, M., Chang, M., Ou, J., Xu, H., Boone, C. and Brown, G. W. (2003) Elg1 forms an alternative RFIC complex important for DNA replication and genome integrity. EMBO J., 22, 4304-4313.
    • (2003) EMBO J. , vol.22 , pp. 4304-4313
    • Bellaoui, M.1    Chang, M.2    Ou, J.3    Xu, H.4    Boone, C.5    Brown, G.W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.