Funktionale Analysen zur SUMOylierung des transkriptionellen Repressors L3MBTL2

L3MBTL2 ist ein Mitglied der Familie von MBT-Domänen Proteinen. MBT-Domänen vermitteln die Bindung an methylierte Lysinreste innerhalb der N-Termini von Histonen. L3MBTL2 wurde als transkriptioneller Repressor beschrieben und ist ein Bestandteil verschiedener Multiproteinkomplexe. In Mäusen besitzt...

Full description

Saved in:
Bibliographic Details
Main Author: Stielow, Christina
Contributors: Suske, Guntram (Prof. Dr.) (Thesis advisor)
Format: Dissertation
Language:German
Published: Philipps-Universität Marburg 2013
Molekularbiologie und Tumorforschung
Subjects:
Online Access:PDF Full Text
Tags: Add Tag
No Tags, Be the first to tag this record!

1. Control of nuclear HIPK2 localization and function by a SUMO interaction motif. Biochimica Et Biophysica Acta 1813, 283–297.


2. Tatham, M.H., Rodriguez, M.S., Xirodimas, D.P., and Hay, R.T. (2009). Detection of protein SUMOylation in vivo. Nature Protocols 4, 1363–1371.


3. Kettlun, A., Uribe, L., Calvo, V., Silva, S., Rivera, J., Mancilla, M., Antonieta, M., Valenzuela, and Traverso-Cori, A. (1982). Properties of two apyrases from Solanum tuberosum. Phytochemistry 21, 551–558.


4. Suske, G. (1999). The Sp-family of transcription factors. Gene 238, 291–300.


5. Stielow, B., Sapetschnig, A., Wink, C., Krüger, I., and Suske, G. (2008b). SUMO- modified Sp3 represses transcription by provoking local heterochromatic gene silencing. EMBO Reports 9, 899–906.


6. Pfander, B., Moldovan, G.-L., Sacher, M., Hoege, C., and Jentsch, S. (2005). SUMO- modified PCNA recruits Srs2 to prevent recombination during S phase. Nature 436, 428–433.


7. Rodriguez, M.S., Dargemont, C., and Hay, R.T. (2001). SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting. The Journal of Biological Chemistry 276, 12654–12659.


8. Sampson, D.A., Wang, M., and Matunis, M.J. (2001). The small ubiquitin-like modifier-1 (SUMO-1) consensus sequence mediates Ubc9 binding and is essential for SUMO-1 modification. The Journal of Biological Chemistry 276, 21664–21669.


9. Complexity of translationally controlled transcription factor Sp3 isoform expression. The Journal of Biological Chemistry 279, 42095–42105.


10. Vlieghe, D., Sandelin, A., De Bleser, P.J., Vleminckx, K., Wasserman, W.W., Van Roy, F., and Lenhard, B. (2006). A new generation of JASPAR, the open-access repository for transcription factor binding site profiles. Nucleic Acids Research 34, D95–7.


11. Schaefer, C.F., Anthony, K., Krupa, S., Buchoff, J., Day, M., Hannay, T., and Buetow, K.H. (2009). PID: the Pathway Interaction Database. Nucleic Acids Research 37, D674–9.


12. Schotta, G., Lachner, M., Sarma, K., Ebert, A., Sengupta, R., Reuter, G., Reinberg, D., and Jenuwein, T. (2004). A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin. Genes & Development 18, 1251–1262.


13. Klymenko, T., Papp, B., Fischle, W., Köcher, T., Schelder, M., Fritsch, C., Wild, B., Wilm, M., and Müller, J. (2006). A Polycomb group protein complex with sequence- specific DNA-binding and selective methyl-lysine-binding activities. Genes & Development 20, 1110–1122.


14. Saunders, A., Werner, J., Andrulis, E.D., Nakayama, T., Hirose, S., Reinberg, D., and Lis, J.T. (2003). Tracking FACT and the RNA polymerase II elongation complex through chromatin in vivo. Science (New York, N.Y.) 301, 1094–1096.


15. Vertegaal, A.C.O., Andersen, J.S., Ogg, S.C., Hay, R.T., Mann, M., and Lamond, A.I. (2006). Distinct and overlapping sets of SUMO-1 and SUMO-2 target proteins revealed by quantitative proteomics. Molecular & Cellular Proteomics 5, 2298–2310.


16. Psakhye, I., and Jentsch, S. (2012). Protein group modification and synergy in the SUMO pathway as exemplified in DNA repair. Cell 151, 807–820.


17. Kouzarides, T. (2007). Chromatin modifications and their function. Cell 128, 693– 705.


18. Sathyamurthy, A., Allen, M.D., Murzin, A.G., and Bycroft, M. (2003). Crystal structure of the malignant brain tumor (MBT) repeats in Sex Comb on Midleg-like 2 (SCML2). The Journal of Biological Chemistry 278, 46968–46973.


19. Vollmer, M. (2005). Der Transkriptionsfaktor Sp3: Etablierung eines zellulären Systems zur Analyse der SUMO-abhängigen Inaktivierung von Sp3, Untersuchungen zur Erythropoiese in Sp1/Sp3-doppeltheterozygoten Mäusen. Diplomarbeit, Fachbereich Medizin der Philipps-Universität Marburg.


20. Ringrose, L., and Paro, R. (2004). Epigenetic regulation of cellular memory by the Polycomb and Trithorax group proteins. Annual Review of Genetics 38, 413–443.


21. FACT, a factor that facilitates transcript elongation through nucleosomes. Cell 92, 105–116.


22. Van der Knaap, J.A., Kumar, B.R.P., Moshkin, Y.M., Langenberg, K., Krijgsveld, J., Heck, A.J.R., Karch, F., and Verrijzer, C.P. (2005). GMP synthetase stimulates histone H2B deubiquitylation by the epigenetic silencer USP7. Molecular Cell 17, 695–707.


23. Pavri, R., Zhu, B., Li, G., Trojer, P., Mandal, S., Shilatifard, A., and Reinberg, D. (2006). Histone H2B monoubiquitination functions cooperatively with FACT to regulate elongation by RNA polymerase II. Cell 125, 703–717.


24. Taverna, S.D., Li, H., Ruthenburg, A.J., Allis, C.D., and Patel, D.J. (2007). How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers. Nature Structural & Molecular Biology 14, 1025–1040.


25. Kahyo, T., Nishida, T., and Yasuda, H. (2001). Involvement of PIAS1 in the sumoylation of tumor suppressor p53. Molecular Cell 8, 713–718.


26. Trojer, P., Li, G., Sims, R.J., Vaquero, A., Kalakonda, N., Boccuni, P., Lee, D., Erdjument-Bromage, H., Tempst, P., Nimer, S.D. et al. (2007). L3MBTL1, a histone- methylation-dependent chromatin lock. Cell 129, 915–928.


27. Sapetschnig, A. (2006). Mechanismen der SUMO-vermittelten Repression am Beispiel des Transkriptionsfaktors Sp3: Identifizierung potentieller Korepressoren. Dissertation, Fachbereich Medizin der Philipps-Universität Marburg.


28. SETDB1: a novel KAP-1-associated histone H3, lysine 9-specific methyltransferase that contributes to HP1-mediated silencing of euchromatic genes by KRAB zinc- finger proteins. Genes & Development 16, 919–932.


29. Tachibana, M., Sugimoto, K., Fukushima, T., and Shinkai, Y. (2001). Set domain- containing protein, G9a, is a novel lysine-preferring mammalian histone methyltransferase with hyperactivity and specific selectivity to lysines 9 and 27 of histone H3. The Journal of Biological Chemistry 276, 25309–25317.


30. Orphanides, G., Wu, W.-H., Lane, W., Hampsey, M., and Reinberg, D. (1999). The chromatin-specific transcription elongation factor FACT comprises human SPT16 and SSRP1 proteins. Nature 400, 284–288.


31. Rischitor, G. (2005). Transcription Factor Sp3 as a target for SUMOylation in vitro. Dissertation, Fachbereich Biologie der Philipps-Universität Marburg.


32. Tatham, M.H., Jaffray, E., Vaughan, O.A., Desterro, J.M., Botting, C.H., Naismith, J.H., and Hay, R.T. (2001). Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9. The Journal of Biological Chemistry 276, 35368–35374.


33. Chromatin deacetylation by an ATP-dependent nucleosome remodelling complex. Nature 395, 917–921.


34. A Drosophila Polycomb group complex includes Zeste and dTAFII proteins. Nature 412, 655–660.


35. Subramanian, A., Tamayo, P., Mootha, V.K., Mukherjee, S., Ebert, B.L., Gillette, M.A., Paulovich, A., Pomeroy, S.L., Golub, T.R., Lander, E.S. et al. (2005). Gene set enrichment analysis: A knowledge-based approach for interpreting genome-wide expression profiles. Proceedings of the National Academy of Sciences of the United States of America 102, 15545–15550.


36. Sapetschnig, A., Rischitor, G., Braun, H., Doll, A., Schergaut, M., Melchior, F., and Suske, G. (2002). Transcription factor Sp3 is silenced through SUMO modification by PIAS1. The EMBO Journal 21, 5206–5215.


37. Krogan, N., Kim, M., Ahn, S., Zhong, G., Kobor, M.S., Cagney, G., Emili, A., Shilatifard, A., Buratowski, S., and Greenblatt, J.F. (2002). RNA polymerase II elongation factors of Saccharomyces cerevisiae: a targeted proteomics approach. Molecular and Cellular Biology 22, 6979–6992.


38. Roseman, R.R., Morgan, K., Mallin, D.R., Roberson, R., Parnell, T.J., Bornemann, D.J., Simon, J.A., and Geyer, P.K. (2001). Long-range repression by multiple polycomb group (PcG) proteins targeted by fusion to a defined DNA-binding domain in Drosophila. Genetics 158, 291–307.


39. Trimarchi, J.M., Fairchild, B., Verona, R., Moberg, K., Andon, N., and Lees, J.A. (1998). E2F-6, a member of the E2F family that can behave as a transcriptional repressor. Proceedings of the National Academy of Sciences of the United States of America 95, 2850–2855.


40. Kerscher, O. (2007). SUMO junction-what's your function? New insights through SUMO-interacting motifs. EMBO Reports 8, 550–555.


41. Characterization of vertebrate cohesin complexes and their regulation in prophase. The Journal of Cell Biology 151, 749–762.


42. Kalakonda, N., Fischle, W., Boccuni, P., Gurvich, N., Hoya-Arias, R., Zhao, X., Miyata, Y., Macgrogan, D., Zhang, J., Sims, J.K. et al. (2008). Histone H4 lysine 20 monomethylation promotes transcriptional repression by L3MBTL1. Oncogene 27, 4293–4304.


43. Sarkari, F., Sanchez-Alcaraz, T., Wang, S., Holowaty, M.N., Sheng, Y., and Frappier, L. (2009). EBNA1-mediated recruitment of a histone H2B deubiquitylating complex to the Epstein-Barr virus latent origin of DNA replication. PLoS Pathogens 5, e1000624.


44. Van der Knaap, J.A., Kozhevnikova, E., Langenberg, K., Moshkin, Y.M., and Verrijzer, C.P. (2010). Biosynthetic enzyme GMP synthetase cooperates with ubiquitin-specific protease 7 in transcriptional regulation of ecdysteroid target genes. Molecular and Cellular Biology 30, 736–744.


45. Qin, J., Buren, D. Van, Huang, H., Zhong, L., Mostoslavsky, R., Akbarian, S., and Hock, H. (2010). Chromatin protein L3mbtl1 is dispensable for development and tumor suppression in mice. Journal of Biological Chemistry 36, 27767–27775.


46. Trojer, P., Cao, A.R., Gao, Z., Li, Y., Zhang, J., Xu, X., Li, G., Losson, R., Erdjument-Bromage, H., Tempst, P. et al. (2011). L3MBTL2 protein acts in concert with PcG protein-mediated monoubiquitination of H2A to establish a repressive chromatin structure. Molecular Cell 42, 438–450.


47. Qin, J., Whyte, W.A., Anderssen, E., Apostolou, E., Chen, H.-H., Akbarian, S., Bronson, R.T., Hochedlinger, K., Ramaswamy, S., Young, R.A. et al. (2012). The Polycomb Group Protein L3mbtl2 Assembles an Atypical PRC1-Family Complex that Is Essential in Pluripotent Stem Cells and Early Development. Cell Stem Cell 2, 1–14.


48. Identification of a SUMO-binding motif that recognizes SUMO-modified proteins. Proceedings of the National Academy of Sciences of the United States of America 101, 14373–14378.


49. Rozenblatt-Rosen, O., Hughes, C., Nannepaga, S., Shanmugam, K.S., Copeland, T.D., Guszczynski, T., Resau, J.H., and Meyerson, M. (2005). The Parafibromin Tumor Suppressor Protein Is Part of a Human Paf1 Complex. Molecular and Cellular Biology 25, 612–620.


50. Kouskouti, A., and Talianidis, I. (2005). Histone modifications defining active genes persist after transcriptional and mitotic inactivation. The EMBO Journal 24, 347–357.


51. A proline-90 residue unique to SUMO-4 prevents maturation and sumoylation. Biochemical and Biophysical Research Communications 337, 517–520.


52. Wang, W.K., Tereshko, V., Boccuni, P., MacGrogan, D., Nimer, S.D., and Patel, D.J. (2003). Malignant Brain Tumor Repeats: A Three-Leaved Propeller Architecture with Ligand/Peptide Binding Pockets. Structure 11, 775–789.


53. Methylation of a histone mimic within the histone methyltransferase G9a regulates protein complex assembly. Molecular Cell 27, 596–608.


54. Stielow, B., Sapetschnig, A., Krüger, I., Kunert, N., Brehm, A., Boutros, M., and Suske, G. (2008a). Identification of SUMO-dependent chromatin-associated transcriptional repression components by a genome-wide RNAi screen. Molecular Cell 29, 742–754.


55. Saether, T., Berge, T., Ledsaak, M., Matre, V., Alm-Kristiansen, A.H., Dahle, O., Aubry, F., and Gabrielsen, O.S. (2007). The chromatin remodeling factor Mi-2alpha acts as a novel co-activator for human c-Myb. The Journal of Biological Chemistry 282, 13994–14005.


56. A human homolog of Drosophila lethal(3)malignant brain tumor (l(3)mbt) protein associates with condensed mitotic chromosomes. Oncogene 18, 3799–3809.