Rocha-Sosa M

Idioma: Español
Referencias bibliográficas: 49
Paginas: 121-131
Archivo PDF: 496.48 Kb.

RESUMEN

La ubicuitina (Ub) es una proteína pequeña la cual es utilizada por los organismos eucariontes para marcar proteínas, en la mayoría de los casos para que éstas sean posteriormente degradadas. La ubicuitinación ocurre en tres pasos sucesivos los cuales requieren de la acción de una enzima activadora, una enzima conjugadora y una ligasa de Ub. Una vez ubicuitinada la proteína seguirá un destino diferente de acuerdo a la topología de la ubicuitinación. Muchas de las proteínas marcadas por ubicuitinación serán degradadas por un complejo proteínico de 2.5 Mda conocido como el proteasoma 26S. Las plantas emplean ampliamente este mecanismo de degradación regulada de proteínas para modular procesos de crecimiento y desarrollo o bien, para responder ante situaciones adversas como puede ser una baja disponibilidad de agua o el ataque por patógenos. Durante la evolución las plantas han desarrollado diversas estrategias para defenderse ante la agresión por patógenos, sin embargo, estos organismos han logrado implementar herramientas que les permiten contrarrestar los mecanismos de defensa de las plantas, entre otras formas, los patógenos han logrado manipular el sistema Ub/proteasoma para poder infectarlas eficientemente.

REFERENCIAS (EN ESTE ARTÍCULO)

1. Atkinson, N.J. & Urwin, P.E. The interaction of plant biotic and abiotic stresses: from genes to the field. J. Exp. Bot. 63, 3523-3544 (2012).

2. Stone, S.L. & Callis, J. Ubiquitin ligases mediate growth and development by promoting protein death. Curr. Opin. Plant Biol. 10, 624 632 (2007).

3. Moon J., Parry, G. & Estelle, M. The ubiquitin-proteasome pathway and plant development. Plant Cell 16, 3181-3195 (2004).

4. Patton, E.E., Willems, A.R. & Tyers, M. Combinatorial control in ubiquitin-dependent proteolysis: don’t Skp the F box hypothesis. Trends Genet. 14, 236 243 (1998).

5. Kornitzer, D. & Ciechanover, A. Modes of regulation of ubiquitin-mediated protein degradation J. Cell Physiol. 182, 1-11 (2000).

6. Goldstein, G. et al. Isolation of a polypeptide that has lymphocytedifferentiating properties and is probably represented universally in living cells. Proc. Natl. Acad. Sci. U.S.A. 72, 11 15 (1975).

7. Woelk, T., Sigismund, S., Penengo, L. & Polo, S. The ubiquitination code: a signalling problem. Cell Div. 2, 11 (2007).

8. Saracco, S.A. et al. Tandem affinity purification and mass spectrometric analysis of ubiquitylated proteins in Arabidopsis. Plant J. 59, 344-358 (2009).

9. Mukhopadhyay, D. & Riezman, H. Proteasome-independent functions of ubiquitin in endocytosis and signaling. Science 315, 201-205 (2007).

10. Ikeda, F. & Dikic, I. Atypical ubiquitin chains: new molecular signals. ‘Protein modifications: Beyond the usual suspects’ review series. EMBO Rep. 9, 536–542 (2008).

11. Deveraux, Q., Ustrell, V., Pickart, C. & Rechsteiner, M. A 26S protease subunit that binds ubiquitin conjugates. J. Biol. Chem. 269, 7059-7061(1994).

12. Nathan, J.A., Kim, H.T., Ting, L., Gygi, S.P. & Goldberg, A.L. Why do cellular proteins linked to K63-polyubiquitin chains not associate with proteasomes? EMBO J. 32, 552-565 (2013).

13. Callis, J., Carpenter, T., Sun, C.W. & Vierstra, R.D. Structure and evolution of genes encoding polyubiquitin and ubiquitin-like proteins in Arabidopsis thaliana ecotype Columbia. Genetics 139, 921-939 (1995).

14. Callis, J. & Vierstra, R.D. Protein degradation in signaling. Curr. Opin. Plant Biol. 3, 381-386 (2000).

15. Hua, Z. & Vierstra, R.D. The cullin-RING ubiquitin-protein ligases. Annu. Rev. Plant Biol. 62, 299-334 (2011).

16. Budhidarmo, R., Nakatani, Y. & Day, C.L. RINGs hold the key to ubiquitin transfer. Trends Biochem. Sci. 37, 58-65 (2012).

17. Nagy, V. & Dikic, I. Ubiquitin ligase complexes: from substrate selectivity to conjugational specificity. Biol. Chem. 391, 163- 169 (2010).

18. Mazzucotelli, E. et al. The e3 ubiquitin ligase gene family in plants: regulation by degradation. Curr. Genomics 7, 509- 522 (2006).

19. Roos-Mattjus, P. & Sistonen, L. The ubiquitin-proteasome pathway. Ann. Med. 36, 285-295 (2004).

20. Kurepa, J. & Smalle, J.A. Structure, function and regulation of plant proteasomes. Biochimie 90, 324-335 (2008).

21. Book, A.J. et al. Affinity purification of the Arabidopsis 26S proteasome reveals a diverse arrays of plant proteolytic complexes. J. Biol. Chem. 285, 25554-25569 (2010).

22. Legget, D.S. et al. Multiple associated proteins regulate proteasome structure and function. Mol. Cell 10, 495-507 (2002).

23. Dodds, P.N. & Rathjen, J.P. Plant immunity: towards an integrated view of plant-pathogen interactions. Nat.Rev. Genet. 11, 539- 548 (2010).

24. Tuda, K. & Katagiri, F. Comparing signaling mechanisms engaged in pattern-triggered and effector-triggered immunity. Curr. Op. Plant Biol. 13, 459-465 (2010).

25. Takizawa, M., Goto, A. & Watanabe, Y. The tobacco ubiquitinactivating enzymes NtE1A and NtE1B are induced by tobacco mosaic virus, wounding and stress hormones. Mol. Cells 19, 228-231 (2005).

26. Maldonado-Calderón, M.T., Sepúlveda-García, E.B. & Rocha- Sosa, M. Characterization of novel F-box proteins in plants induced by biotic and abiotic stress. Plant Sci. 185-186, 208- 217 (2012).

27. Salinas-Mondragón, R.E., Garciadueñas-Piña, C. & Guzmán, P. Early elicitor induction in members of a novel multigene family coding for highly related RING-H2 proteins in Arabidopsis thaliana. Plant Mol. Biol. 40, 579-590 (1999).

28. Suty, L. et al. Preferential induction of 20S proteasome subunits during elicitation of plant defense reactions: towards the characterization of “plant defense proteasomes”. Int. J. Biochem. Cell Biol. 35, 637-650 (2003).

29. Goritschnig, S., Zhang, Y. & Li, X. The ubiquitin pathway is required for innate immunity in Arabidopsis. Plant J. 49, 540-551 (2007).

30. Cao, Y. et al. Overexpression of a rice defense-related F-box protein gene OsDRF1 in tobacco improves disease resistance through potentiation of defense gene expression. Physiol. Plant 134, 440-452 (2008).

31. van den Burg, H.A. et al. The F-box protein ACRE189/ACIF1 regulates cell death and defense responses activated during pathogen recognition intobacco and tomato. Plant Cell 20, 697-719 (2008).

32. Lee, D.H., Choi, H.W. & Hwang, B.K. The pepper E3 ubiquitin ligase RING1 gene, CaRING1, is required for cell death and the salicylic acid-dependent defense response. Plant Physiol. 156, 2011-2025 (2011).

33. Lin, S.S. et al. RING1 E3 ligase localizes to plasma membrane lipid rafts to trigger FB1-induced programmed cell death in Arabidopsis. Plant J. 56, 550-561 (2008).

34. Luo, H. et al. The Arabidopsis botrytis Susceptible1 Interactor defines a subclass of RING E3 ligases that regulate pathogen and stress responses. Plant Physiol. 154, 1766-1782 (2010).

35. Cheng, Y.T. et al. Stability of plant immune-receptor resistance proteins is controlled by SKP1-CULLIN-F-box (SCF)- mediated protein degradation. Proc. Natl. Acad. Sci. U.S.A. 108, 14694-14699 (2011).

36. Gou, M. et al. The F-box protein CPR1/CPR30 negatively regulates R protein SNC1 accumulation. Plant J. 69, 411- 420 (2012).

37. Marino, D. et al. Arabidopsis ubiquitin ligase MIEL1 mediates degradation of the transcription factor MYB30 weakening plant defence. Nature Comms. 4, 1476 (2013).

38. Lu, D. et al. Direct ubiquitination of pattern recognition receptor FLS2 attenuates plant innate immunity. Science 332, 1439- 1442 (2011).

39. Robatzek, S., Chinchilla, D. & Boller, T. Ligand-induced endocytosis of the pattern recognition receptor FLS2 in Arabidopsis. Genes Dev. 20, 537-542 (2006).

40. Trujillo, M., Ichimura, K., Casais, C. & Shirasu, K. Negative regulation of PAMP-triggered immunity by an E3 ubiquitin ligase triplet in Arabidopsis. Curr. Biol. 18, 1396-1401(2008).

41. Stegmann, M. et al. The ubiquitin ligase PUB22 targets a subunit of the exocyst complex required for PAMP-triggered responses in Arabidopsis. Plant Cell 24, 4703-4716 (2012).

42. Groll, M. et al. A plant pathogen virulence factor inhibits the eukaryotic proteasome by a novel mechanism. Nature 452, 755-758 (2008).

43. Reichel, C. & Beachy, R.N. Degradation of tobacco mosaic virus movement protein by the 26S proteasome. J. Virol. 74, 3330- 3337 (2000).

44. Bos, J.I. et al. Phytophthora infestans effector AVR3a is essential for virulence and manipulates plant immunity by stabilizing host E3 ligase CMPG1. Proc. Natl. Acad. Sci. U.S.A. 107, 9909-9914 (2010).

45. Chronis, D. et al. A ubiquitin carboxyl extension protein secreted from a plantparasitic nematode Globodera rostochiensis is cleaved in planta to promote plant parasitism. Plant J. 74, 185-196 (2013).

46. Janjusevic, R., Abramovitch, R.B., Martin, G.B. & Stebbins, C.E. A bacterial inhibitor of host programmed cell death defenses is an E3 ubiquitin ligase. Science 311, 222-226 (2006).

47. Rosebrock, T.R. et al. A bacterial E3 ubiquitin ligase targets a host protein kinase to disrupt plant immunity. Nature 448, 370-374 (2007).

48. Göhre, V. et al. Plant pattern-recognition receptor FLS2 is directed for degradation by the bacterial ubiquitin ligase AvrPtoB. Curr. Biol. 18, 1824-1832 (2008).

49. Tzfira, T., Vaidya, M. & Citovsky, V. Involvement of targeted proteolysis in plant genetic transformation by Agrobacterium. Nature 431, 87-92 (2004).