Diversity of the SUMOylation machinery in plants

Biochemical Society Transactions

Volumn 38, Issue 1, 2010, Pages 60-64

  Lois, L Maria ^a  

^a CSIC   (Spain)

Author keywords

Arabidopsis; Conjugation machinery; Plant; Protein target; Small ubiquitin related modifier (SUMO)

Indexed keywords

PROTEINASE; SUMO 1 PROTEIN; SUMO 2 PROTEIN; SUMO 3 PROTEIN; SUMO 5 PROTEIN; SUMO PROTEIN; UBIQUITIN LIKE PROTEASE; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

ARABIDOPSIS; CELLULAR DISTRIBUTION; CONJUGATION; EXPRESSED SEQUENCE TAG; MOLECULAR PHYLOGENY; NONHUMAN; PLANT DEVELOPMENT; PLANT GENOME; PLANT GROWTH; PRIORITY JOURNAL; REVIEW; SUMOYLATION;

ARABIDOPSIS; ARABIDOPSIS PROTEINS; MOLECULAR SEQUENCE DATA; PHYLOGENY; PROTEIN PROCESSING, POST-TRANSLATIONAL; SMALL UBIQUITIN-RELATED MODIFIER PROTEINS;

ARABIDOPSIS; EUKARYOTA;

EID: 76449110686     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST0380060     Document Type: Review

References (35)

1. Melchior, F. (2000) SUMO: nonclassical ubiquitin. Annu. Rev. Cell Dev. Biol. 16, 591-626
2. Johnson, E.S. (2004) Protein modification by SUMO. Annu. Rev. Biochem. 73, 355-382
3. Lois, L.M. and Lima, C.D. (2005) Structures of the SUMO E1 provide mechanistic insights into SUMO activation and E2 recruitment to E1. EMBO J. 24, 439-451
4. Yunus, A.A. and Lima, C.D. (2006) Lysine activation and functional analysis of E2-mediated conjugation in the SUMO pathway. Nat. Struct. Mol. Biol. 13, 491-499
5. Capili, A.D. and Lima, C.D. (2007) Structure and analysis of a complex between SUMO and Ubc9 illustrates features of a conserved E2-Ubl interaction. J. Mol. Biol. 369, 608-618
6. Dye, B.T. and Schulman, B.A. (2007) Structural mechanisms underlying posttranslational modification by ubiquitin-like proteins. Annu. Rev. Biophys. Biomol. Struct. 36, 131-150
7. Knipscheer, P., van Dijk, W.J., Olsen, J.V., Mann, M. and Sixma, T.K. (2007) Noncovalent interaction between Ubc9 and SUMO promotes SUMO chain formation. EMBO J. 26, 2797-2807
8. Mukhopadhyay, D. and Dasso, M. (2007) Modification in reverse: the SUMO proteases. Trends Biochem. Sci. 32, 286-295
9. Lois, L.M., Lima, C.D. and Chua, N.H. (2003) Small ubiquitin-like modifier modulates abscisic acid signaling in Arabidopsis. Plant Cell 15, 1347-1359
10. Murtas, G., Reeves, P.H., Fu, Y.F., Bancroft, I., Dean, C. and Coupland, G. (2003) A nuclear protease required for flowering-time regulation in Arabidopsis reduces the abundance of SMALL UBIQUITIN-RELATED MODIFIER conjugates. Plant Cell 15, 2308-2319
11. Miura, K., Rus, A., Sharkhuu, A., Yokoi, S., Karthikeyan, A.S., Raghothama, K.G., Baek, D., Koo, Y.D., Jin, J.B., Bressan, R.A. et al. (2005) The Arabidopsis SUMO E3 ligase SIZ1 controls phosphate deficiency responses. Proc. Natl. Acad. Sci. U.S.A. 102, 7760-7765
12. Colby, T., Matthai, A., Boeckelmann, A. and Stuible, H.P. (2006) SUMO-conjugating and SUMO-deconjugating enzymes from Arabidopsis. Plant Physiol. 142, 318-332
13. Chosed, R., Mukherjee, S., Lois, L.M. and Orth, K. (2006) Evolution of a signalling system that incorporates both redundancy and diversity: Arabidopsis SUMOylation. Biochem. J. 398, 521-529
14. Budhiraja, R., Hermkes, R., Muller, S., Schmidt, J., Colby, T., Panigrahi, K., Coupland, G. and Bachmair, A. (2009) Substrates related to chromatin and to RNA-dependent processes are modified by Arabidopsis SUMO isoforms that differ in a conserved residue with influence on desumoylation. Plant Physiol. 149, 1529-1540
15. Kurepa, J., Walker, J.M., Smalle, J., Gosink, M.M., Davis, S.J., Durham, T.L., Sung, D.Y. and Vierstra, R.D. (2003) The small ubiquitin-like modifier (SUMO) protein modification system in Arabidopsis: accumulation of SUMO1 and -2 conjugates is increased by stress. J. Biol. Chem. 278, 6862-6872
16. Dohmen, R.J., Stappen, R., McGrath, J.P., Forrova, H., Kolarov, J., Goffeau, A. and Varshavsky, A. (1995) An essential yeast gene encoding a homolog of ubiquitin-activating enzyme. J. Biol. Chem. 270, 18099-18109
17. Pichler, A., Gast, A., Seeler, J.S., Dejean, A. and Melchior, F. (2002) The nucleoporin RanBP2 has SUMO1 E3 ligase activity. Cell 108, 109-120
18. Chosed, R., Tomchick, D.R., Brautigam, C.A., Mukherjee, S., Negi, V.S., Machius, M. and Orth, K. (2007) Structural analysis of Xanthomonas XopD provides insights into substrate specificity of ubiquitin-like protein proteases. J. Biol. Chem. 282, 6773-6782
19. Meulmeester, E., Kunze, M., Hsiao, H.H., Urlaub, H. and Melchior, F. (2008) Mechanism and consequences for paralog-specific sumoylation of ubiquitin-specific protease 25. Mol. Cell. 30, 610-619
20. Zhang, F.P., Mikkonen, L., Toppari, J., Palvimo, J.J., Thesleff, I. and Janne, O.A. (2008) SUMO-1 function is dispensable in normal mouse development. Mol. Cell. Biol. 28, 5381-5390
21. Evdokimov, E., Sharma, P., Lockett, S.J., Lualdi, M. and Kuehn, M.R. (2008) Loss of SUMO1 in mice affects RanGAP1 localization and formation of PML nuclear bodies, but is not lethal as it can be compensated by SUMO2 or SUMO3. J. Cell Sci. 121, 4106-4113
22. Saracco, S.A., Miller, M.J., Kurepa, J. and Vierstra, R.D. (2007) Genetic analysis of SUMOylation in Arabidopsis: conjugation of SUMO1 and SUMO2 to nuclear proteins is essential. Plant Physiol. 145, 119-134
23. Hruz, T., Laule, O., Szabo, G., Wessendorp, F., Bleuler, S., Oertle, L., Widmayer, P., Gruissem, W. and Zimmermann, P. (2008) Genevestigator V3: a reference expression database for the meta-analysis of transcriptomes. Adv. Bioinformatics 2008, 420747
24. Reverter, D. and Lima, C.D. (2006) Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates. Nat. Struct. Mol. Biol. 13, 1060-1068
25. Conti, L., Price, G., O'Donnell, E., Schwessinger, B., Dominy, P. and Sadanandom, A. (2008) Small ubiquitin-like modifier proteases OVERLY TOLERANT TO SALT1 and -2 regulate salt stress responses in Arabidopsis. Plant Cell 20, 2894-2908
26. Ishida, T., Fujiwara, S., Miura, K., Stacey, N., Yoshimura, M., Schneider, K., Adachi, S., Minamisawa, K., Umeda, M. and Sugimoto, K. (2009) SUMO E3 Ligase HIGH PLOIDY2 regulates endocycle onset and meristem maintenance in Arabidopsis. Plant Cell 21, 2284-2297
27. Miura, K., Lee, J., Jin, J.B., Yoo, C.Y., Miura, T. and Hasegawa, P.M. (2009) Sumoylation of ABI5 by the Arabidopsis SUMO E3 ligase SIZ1 negatively regulates abscisic acid signaling. Proc. Natl. Acad. Sci. U.S.A. 106, 5418-5423
28. Jin, J.B., Jin, Y.H., Lee, J., Miura, K., Yoo, C.Y., Kim, W.Y., Van Oosten, M., Hyun, Y., Somers, D.E., Lee, I. et al. (2008) The SUMO E3 ligase, AtSIZ1, regulates flowering by controlling a salicylic acid-mediated floral promotion pathway and through affects on FLC chromatin structure. Plant J. 53, 530-540
29. Miura, K., Jin, J.B., Lee, J., Yoo, C.Y., Stirm, V., Miura, T., Ashworth, E.N., Bressan, R.A., Yun, D.J. and Hasegawa, P.M. (2007) SIZ1-mediated sumoylation of ICE1 controls CBF3/DREB1A expression and freezing tolerance in Arabidopsis. Plant Cell 19, 1403-1414
30. Garcia-Dominguez, M., March-Diaz, R. and Reyes, J.C. (2008) The PHD domain of plant PIAS proteins mediates sumoylation of bromodomain GTE proteins. J. Biol. Chem. 283, 21469-21477
31. Yoo, C.Y., Miura, K., Jin, J.B., Lee, J., Park, H.C., Salt, D.E., Yun, D.J., Bressan, R.A. and Hasegawa, P.M. (2006) SIZ1 SUMO E3 ligase facilitates basal thermotolerance in Arabidopsis independent of salicylic acid. Plant Physiol. 142, 1548-1558
32. Catala, R., Ouyang, J., Abreu, I.A., Hu, Y., Seo, H., Zhang, X. and Chua, N.H. (2007) The Arabidopsis E3 SUMO ligase SIZ1 regulates plant growth and drought responses. Plant Cell 19, 2952-2966
33. Lee, J., Nam, J., Park, H.C., Na, G., Miura, K., Jin, J.B., Yoo, C.Y., Baek, D., Kim, D.H., Jeong, J.C. et al. (2007) Salicylic acid-mediated innate immunity in Arabidopsis is regulated by SIZ1 SUMO E3 ligase. Plant J. 49, 79-90
34. Edgar, R.C. (2004) MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res. 32, 1792-1797
35. Mossessova, E. and Lima, C.D. (2000) Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast. Mol. Cell 5, 865-876