Recognition of SUMO-modified PCNA requires tandem receptor motifs in Srs2 (original) (raw)
Kirkin, V. & Dikic, I. Role of ubiquitin- and Ubl-binding proteins in cell signaling. Curr. Opin. Cell Biol.19, 199–205 (2007) ArticleCASPubMed Google Scholar
Gareau, J. R. & Lima, C. D. The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition. Nature Rev. Mol. Cell Biol.11, 861–871 (2010) ArticleCAS Google Scholar
Dikic, I., Wakatsuki, S. & Walters, K. J. Ubiquitin-binding domains – from structures to functions. Nature Rev. Mol. Cell Biol.10, 659–671 (2009) ArticleCAS Google Scholar
Moldovan, G. L., Pfander, B. & Jentsch, S. PCNA, the maestro of the replication fork. Cell129, 665–679 (2007) ArticleCASPubMed Google Scholar
Krishna, T. S., Kong, X. P., Gary, S., Burgers, P. M. & Kuriyan, J. Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA. Cell79, 1233–1243 (1994) ArticleCASPubMed Google Scholar
Gulbis, J. M., Kelman, Z., Hurwitz, J., O’Donnell, M. & Kuriyan, J. Structure of the C-terminal region of p21(WAF1/CIP1) complexed with human PCNA. Cell87, 297–306 (1996) ArticleCASPubMed Google Scholar
Bruning, J. B. & Shamoo, Y. Structural and thermodynamic analysis of human PCNA with peptides derived from DNA polymerase-δ p66 subunit and flap endonuclease-1. Structure12, 2209–2219 (2004) ArticleCASPubMed Google Scholar
Vijayakumar, S. et al. The C-terminal domain of yeast PCNA is required for physical and functional interactions with Cdc9 DNA ligase. Nucleic Acids Res.35, 1624–1637 (2007) ArticleCASPubMedPubMed Central Google Scholar
Scott, M. T., Morrice, N. & Ball, K. L. Reversible phosphorylation at the C-terminal regulatory domain of p21(Waf1/Cip1) modulates proliferating cell nuclear antigen binding. J. Biol. Chem.275, 11529–11537 (2000) ArticleCASPubMed Google Scholar
Hoege, C., Pfander, B., Moldovan, G. L., Pyrowolakis, G. & Jentsch, S. RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature419, 135–141 (2002) ArticleADSCASPubMed Google Scholar
Stelter, P. & Ulrich, H. D. Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugation. Nature425, 188–191 (2003) ArticleADSCASPubMed Google Scholar
Pfander, B., Moldovan, G. L., Sacher, M., Hoege, C. & Jentsch, S. SUMO-modified PCNA recruits Srs2 to prevent recombination during S phase. Nature436, 428–433 (2005) ArticleADSCASPubMed Google Scholar
Papouli, E. et al. Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p. Mol. Cell19, 123–133 (2005) ArticleCASPubMed Google Scholar
Krejci, L. et al. DNA helicase Srs2 disrupts the Rad51 presynaptic filament. Nature423, 305–309 (2003) ArticleADSCASPubMed Google Scholar
Veaute, X. et al. The Srs2 helicase prevents recombination by disrupting Rad51 nucleoprotein filaments. Nature423, 309–312 (2003) ArticleADSCASPubMed Google Scholar
Lawrence, C. W. & Christensen, R. B. Metabolic suppressors of trimethoprim and ultraviolet light sensitivities of Saccharomyces cerevisiaerad6 mutants. J. Bacteriol.139, 866–876 (1979) CASPubMedPubMed Central Google Scholar
Baba, D. et al. Crystal structure of thymine DNA glycosylase conjugated to SUMO-1. Nature435, 979–982 (2005) ArticleADSCASPubMed Google Scholar
Ulrich, H. D. PCNASUMO and Srs2: a model SUMO substrate-effector pair. Biochem. Soc. Trans.35, 1385–1388 (2007) ArticleCASPubMed Google Scholar
Song, J., Durrin, L. K., Wilkinson, T. A., Krontiris, T. G. & Chen, Y. Identification of a SUMO-binding motif that recognizes SUMO-modified proteins. Proc. Natl Acad. Sci. USA101, 14373–14378 (2004) ArticleADSCASPubMedPubMed Central Google Scholar
Chang, C. C. et al. Structural and functional roles of Daxx SIM phosphorylation in SUMO paralog-selective binding and apoptosis modulation. Mol. Cell42, 62–74 (2011) ArticleCASPubMed Google Scholar
Hishiki, A. et al. Structural basis for novel interactions between human translesion synthesis polymerases and proliferating cell nuclear antigen. J. Biol. Chem.284, 10552–10560 (2009) ArticleCASPubMedPubMed Central Google Scholar
Yunus, A. A. & Lima, C. D. Structure of the Siz/PIAS SUMO E3 ligase Siz1 and determinants required for SUMO modification of PCNA. Mol. Cell35, 669–682 (2009) ArticleCASPubMedPubMed Central Google Scholar
Yunus, A. A. & Lima, C. D. Purification of SUMO conjugating enzymes and kinetic analysis of substrate conjugation. Methods Mol. Biol.497, 167–186 (2009) ArticleCASPubMedPubMed Central Google Scholar
Freudenthal, B. D., Brogie, J. E., Gakhar, L., Kondratick, C. M. & Washington, M. T. Crystal structure of SUMO-modified proliferating cell nuclear antigen. J. Mol. Biol.406, 9–17 (2011) ArticleCASPubMed Google Scholar
Kazmirski, S. L., Zhao, Y., Bowman, G. D., O’Donnell, M. & Kuriyan, J. Out-of-plane motions in open sliding clamps: molecular dynamics simulations of eukaryotic and archaeal proliferating cell nuclear antigen. Proc. Natl Acad. Sci. USA102, 13801–13806 (2005) ArticleADSCASPubMedPubMed Central Google Scholar
Miyata, T. et al. Open clamp structure in the clamp-loading complex visualized by electron microscopic image analysis. Proc. Natl Acad. Sci. USA102, 13795–13800 (2005) ArticleADSCASPubMedPubMed Central Google Scholar
Bowman, G. D., O’Donnell, M. & Kuriyan, J. Structural analysis of a eukaryotic sliding DNA clamp–clamp loader complex. Nature429, 724–730 (2004) ArticleADSCASPubMed Google Scholar
Sakurai, S. et al. Structural basis for recruitment of human flap endonuclease 1 to PCNA. EMBO J.24, 683–693 (2005) ArticleCASPubMed Google Scholar
Baba, D. et al. Crystal structure of SUMO-3-modified thymine-DNA glycosylase. J. Mol. Biol.359, 137–147 (2006) ArticleCASPubMed Google Scholar
Olsen, S. K., Capili, A. D., Lu, X., Tan, D. S. & Lima, C. D. Active site remodelling accompanies thioester bond formation in the SUMO E1. Nature463, 906–912 (2010) ArticleADSCASPubMedPubMed Central Google Scholar
Song, J., Zhang, Z., Hu, W. & Chen, Y. Small ubiquitin-like modifier (SUMO) recognition of a SUMO binding motif: a reversal of the bound orientation. J. Biol. Chem.280, 40122–40129 (2005) ArticleCASPubMed Google Scholar
Sekiyama, N. et al. Structure of the small ubiquitin-like modifier (SUMO)-interacting motif of MBD1-containing chromatin-associated factor 1 bound to SUMO-3. J. Biol. Chem.283, 35966–35975 (2008) ArticleCASPubMed Google Scholar
Moldovan, G. L., Pfander, B. & Jentsch, S. PCNA controls establishment of sister chromatid cohesion during S phase. Mol. Cell23, 723–732 (2006) ArticleCASPubMed Google Scholar
Seet, B. T., Dikic, I., Zhou, M. M. & Pawson, T. Reading protein modifications with interaction domains. Nature Rev. Mol. Cell Biol.7, 473–483 (2006) ArticleCAS Google Scholar
Bienko, M. et al. Ubiquitin-binding domains in Y-family polymerases regulate translesion synthesis. Science310, 1821–1824 (2005) ArticleADSCASPubMed Google Scholar
Chen, J., Ai, Y., Wang, J., Haracska, L. & Zhuang, Z. Chemically ubiquitylated PCNA as a probe for eukaryotic translesion DNA synthesis. Nature Chem. Biol.6, 270–272 (2010) ArticleCAS Google Scholar
Moldovan, G. L. et al. Inhibition of homologous recombination by the PCNA-interacting protein PARI. Mol. Cell45, 75–86 (2012) ArticleCASPubMed Google Scholar
Mossessova, E. & Lima, C. D. Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast. Mol. Cell5, 865–876 (2000) ArticleCASPubMed Google Scholar
Rayment, I. Reductive alkylation of lysine residues to alter crystallization properties of proteins. Methods Enzymol.276, 171–179 (1997) ArticleCASPubMed Google Scholar
Otwinowski, Z. & Minor, W. in Methods in Enzymology vol. 276 (eds Carter, C. W. Jr. & Sweet, R. M. ) 307–326 (Academic Press, 1997) Google Scholar
Collaborative Computational Project. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D50, 760–763 (1994)
Vagin, A. & Teplyakov, A. MOLREP: an automated program from molecular replacement. J. Appl. Crystallogr.30, 1022–1025 (1997) ArticleCAS Google Scholar
Jones, T. A., Zou, J. Y., Cowan, S. W. & Kjeldgaard, M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47, 110–119 (1991) ArticlePubMed Google Scholar
Murshudov, G. N., Vagin, A. A. & Dodson, E. J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D53, 240–255 (1997) ArticleCASPubMed Google Scholar
Chen, V. B. et al. MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr. D66, 12–21 (2010) ArticleCASPubMed Google Scholar
Delano, W. The PyMOL Molecular Graphics System (DeLano Scientific, 2002)