Ring1B contains a ubiquitin-like docking module for interaction with Cbx proteins

Biochemistry

Volumn 48, Issue 44, 2009, Pages 10542-10548

  Bezsonova, Irina ^a,b   Walker, John R ^a   Bacik, John P ^a   Duan, Shili ^b   Dhe Paganon, Sirano ^a   Arrowsmith, Cheryl H ^a,b  

^a UNIVERSITY OF TORONTO   (Canada)

^b UNIVERSITY OF TORONTO   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE COMPLEXES; C-TERMINAL DOMAINS; COMPLEX 1; EPIGENETIC MODIFICATION; HIGH-RESOLUTION STRUCTURES; HOMODIMERS; MUTATIONAL ANALYSIS; NUCLEOSOMES; POLYCOMB; POLYCOMB GROUP; RNA BINDING; SURFACE REGION; UBIQUITIN-LIKE; UBIQUITYLATION;

CHROMOSOMES; NUCLEIC ACIDS; RNA; TRANSCRIPTION; TRANSCRIPTION FACTORS;

CRYSTAL STRUCTURE;

CBX PROTEIN; MEMBRANE PROTEIN; POLYCOMB GROUP PROTEIN; RING 1 B PROTEIN; UBIQUITIN; UNCLASSIFIED DRUG;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CRYSTAL STRUCTURE; MUTATIONAL ANALYSIS; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; CELLS, CULTURED; CRYSTALLOGRAPHY, X-RAY; CULTURE MEDIA; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; REPRESSOR PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SURFACE PLASMON RESONANCE; UBIQUITIN;

EID: 70449453475     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi901131u     Document Type: Article

References (34)

1. Schwartz, Y. B., and Pirrotta, V. (2008) Polycomb complexes and epigenetic states. Curr. Opin. Cell. Biol. 20, 266-273.
2. Shukla, A., Chaurasia, P., and Bhaumik, S. R. (2009) Histone methylation and ubiquitination with their cross-talk and roles in gene expression and stability. Cell. Mol. Life Sci. 66, 1419-1433.
3. Wang, H., Wang, L., Erdjument-Bromage, H., Vidal, M., Tempst, P., Jones, R. S., and Zhang, Y. (2004) Role of histone H2A ubiquitination in Polycomb silencing. Nature 431, 873-878. (Pubitemid 39434086)
4. Kuzmichev, A., Nishioka, K., Erdjument-Bromage, H., Tempst, P., and Reinberg, D. (2002) Histone methyltransferase activity associated with a human multiprotein complex containing the Enhancer of Zeste protein. Genes Dev. 16, 2893-2905.
5. Cao, R., Tsukada, Y., and Zhang, Y. (2005) Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing. Mol. Cell 20, 845-854. (Pubitemid 41814874)
6. Zhou, W., Zhu, P., Wang, J., Pascual, G., Ohgi, K. A., Lozach, J., Glass, C. K., and Rosenfeld, M. G. (2008) Histone H2A monoubiquitination represses transcription by inhibiting RNA polymerase II transcriptional elongation. Mol. Cell 29, 69-80.
7. Bernstein, E., Duncan, E. M., Masui, O., Gil, J., Heard, E., and Allis, C. D. (2006) Mouse polycomb proteins bind differentially to methylated histone H3 and RNA and are enriched in facultative heterochromatin. Mol. Cell. Biol. 26, 2560-2569.
8. Vincenz, C., and Kerppola, T. K. (2008) Different polycomb group CBX family proteins associate with distinct regions of chromatin using nonhomologous protein sequences. Proc. Natl. Acad. Sci. U.S.A. 105, 16572-16577.
9. Han, Z., Xing, X., Hu, M., Zhang, Y., Liu, P., and Chai, J. (2007) Structural basis of EZH2 recognition by EED. Structure 15, 1306-1315. (Pubitemid 47539160)
10. Buchwald, G., van der Stoop, P., Weichenrieder, O., Perrakis, A., van Lohuizen, M., and Sixma, T. K. (2006) Structure and E3-ligase activity of the Ring-Ring complex of polycomb proteins Bmi1 and Ring1b. EMBO J. 25, 2465-2474. (Pubitemid 44012229)
11. Li, Z., Cao, R., Wang, M., Myers, M. P., Zhang, Y., and Xu, R. M. (2006) Structure of a Bmi-1-Ring1B polycomb group ubiquitin ligase complex. J. Biol. Chem. 281, 20643-20649.
12. Sanchez-Pulido, L., Devos, D., Sung, Z. R., and Calonje, M. (2008) RAWUL: A new ubiquitin-like domain in PRC1 ring finger proteins that unveils putative plant and worm PRC1 orthologs. Bmc Genomics 9, 308-318.
13. Czypionka, A., de los Panos, O. R., Mateu, M. G., Barrera, F. N., Hurtado-Gomez, E., Gomez, J., Vidal, M., and Neira, J. L. (2007) The isolated C-terminal domain of Ring1B is a dimer made of stable, well-structured monomers. Biochemistry 46, 12764-12776.
14. Wang, R. J., Ilangovan, U., Robinson, A. K., Schirf, V., Schwarz, P. M., Lafer, E. M., Demeler, B., Hinck, A. P., and Kim, C. A. (2008) Structural transitions of the RING1BC-terminal region upon binding the polycomb cbox domain. Biochemistry 47, 8007-8015.
15. Schoorlemmer, J., MarcosGutierrez, C., Were, F., Martinez, R., Garcia, E., Satijn, D. P. E., Otte, A. P., and Vidal, M. (1997) Ring1A is a transcriptional repressor that interacts with the Polycomb-M33 protein and is expressed at rhombomere boundaries in the mouse hindbrain. EMBO J. 16, 5930-5942.
16. Minor, W., Cymborowski, M., and Otwinowski, Z. (2002) Automatic system for crystallographic data collection and analysis. Acta Phys. Pol., A 101, 613-619.
17. Terwilliger, T. C. (2003) SOLVE and RESOLVE: automated structure solution and density modification. Methods Enzymol. 374, 22-37.
18. Cohen, S. X., Ben Jelloul, M., Long, F., Vagin, A., Knipscheer, P., Lebbink, J., Sixma, T. K., Lamzin, V. S., Murshudov, G. N., and Perrakis, A. (2008) ARP/wARP and molecular replacement: the next generation. Acta Crystallogr., Sect. D: Biol. Crystallogr. 64, 49-60.
19. Emsley, P., and Cowtan, K. (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr., Sect. D: Biol. Crystallogr. 60, 2126-2132.
20. Winn, M. D., Murshudov, G. N., and Papiz, M. Z. (2003) Macromolecular TLS refinement in REFMAC at moderate resolutions. Methods Enzymol. 374, 300-321.
21. Painter, J., and Merritt, E. A. (2006) TLSMD web server for the generation of multi-group TLS models. J. Appl. Crystallogr. 39, 109-111.
22. Painter, J., and Merritt, E. A. (2006) Optimal description of a protein structure in terms of multiple groups undergoing TLS motion. Acta Crystallogr., Sect. D: Biol. Crystallogr. 62, 439-450.
23. Lo, M. C., Aulabaugh, A., Jin, G., Cowling, R., Bard, J., Malamas, M., and Ellestad, G. (2004) Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery. Anal. Biochem. 332, 153-159.
24. Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293.
25. Johnson, B. A. (2004) Using NMRView to visualize and analyze the NMR spectra of macromolecules. Methods Mol. Biol. 278, 313-352.
26. Davis, I. W., Leaver-Fay, A., Chen, V. B., Block, J. N., Kapral, G. J., Wang, X., Murray, L. W., Arendall, W. B.III, Snoeyink, J., Richardson, J. S., and Richardson, D. C. (2007) MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res. 35, W375-W383.
27. Davis, I. W., Murray, L. W., Richardson, J. S., and Richardson, D. C. (2004) MOLPROBITY: structure validation and all-atom contact analysis for nucleic acids and their complexes. Nucleic Acids Res. 32, W615-W619.
28. Jentsch, S., and Pyrowolakis, G. (2000) Ubiquitin and its kin: how close are the family ties? Trends Cell Biol. 10, 335-342.
29. Holm, L., Kaariainen, S., Rosenstrom, P., and Schenkel, A. (2008) Searching protein structure databases with DaliLite v.3. Bioinformatics 24, 2780-2781. (Pubitemid 352722625)
30. Cecconi, F., and Levine, B. (2008) The role of autophagy in mammalian development: cell makeover rather than cell death. Dev. Cell 15, 344-357.
31. Hashimoto, H., Horton, J. R., Zhang, X., and Cheng, X. (2009) UHRF1, a modular multidomain protein, regulates replication-coupled crosstalk between DNA methylation and histone modifications. Epigenetics 4, 8-14.
32. Moore, D. J. (2006) Parkin: a multifaceted ubiquitin ligase. Biochem. Soc. Trans. 34, 749-753
33. Neira, J. L., Roman-Trufero, M., Contreras, L. M., Prieto, J., Singh, G., Barrera, F. N., Renart, M. L., and Vidal, M. (2009) The Transcriptional Repressor RYBP Is a Natively Unfolded Protein Which Folds upon Binding to DNA (dagger). Biochemistry 48 (6), 1348-1360.
34. Krissinel, E., and Henrick, K. (2007) Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774-797.