جلد 10، شماره 1 - ( (پاییز و زمستان) 1399 )
جلد 10 شماره 1 صفحات 152-141 |
برگشت به فهرست نسخه ها
Download citation:
BibTeX | RIS | EndNote | Medlars | ProCite | Reference Manager | RefWorks
Send citation to:
BibTeX | RIS | EndNote | Medlars | ProCite | Reference Manager | RefWorks
Send citation to:
Tahmasebi A. (2021). The role of ubiquitin in plant-virus interactions. Plant Pathol. Sci.. 10(1), 141-152. doi:10.52547/pps.10.1.141
URL: http://yujs.yu.ac.ir/pps/article-1-333-fa.html
URL: http://yujs.yu.ac.ir/pps/article-1-333-fa.html
طهماسبی امین الله. نقش یوبیکوئیتین در برهمکنش‌های ویروس-گیاه دانش بیماری شناسی گیاهی 1399; 10 (1) :152-141 10.52547/pps.10.1.141
گروه کشاورزی، مجتمع آموزش عالی میناب، دانشگاه هرمزگان ، Tahmasebi.info@yahoo.com
چکیده: (5242 مشاهده)
طهماسبی ا (1399) نقش یوبیکوئیتین در برهمکنش‌های ویروس-گیاه. دانش بیماری‌شناسی گیاهی 10(1): 152-141. Doi: 10.2982/PPS.10.1.141.
ویروسهای گیاهی باعث خسارت عمده به محصولات کشاورزی در سراسر دنیا میشوند. گیاهان از طریق چندین سازوکار دفاعی نظیر یوبیکوئیتین به آلودگیهای ویروسی پاسخ میدهند. یوبیکوئیتین و سیستم یوبیکوئیتین پروتئازوم نقش مهمی در تغییر عملکرد و تجزیه پروتئین در گیاهان ایفا میکنند. اتصال یوبی-کوئیتین به پروتئینهای سلولی باعث تغییر در پایداری، استقرار سلولی و یا فعالیت پروتئین هدف میشود. نقش مهم سیستم یوبیکوئیتین پروتئازوم در سازوکارهای دفاعی و سایر فرایندهای گیاه نیز مشخص شده است. ویروسها به عنوان انگلهای اجباری درون سلولی، سازوکارهایی را در جهت تداخل و یا استفاده از سیستم یوبیکوئیتین پروتئازوم تکامل داده اند. در مواردی هم ممکن است پروتئینهای ویروسی توسط سیستم یوبیکوئیتین پروتئازوم مورد هدف قرار گیرند. یوبی کوئیتینه شدن پروتئینها نقش مهمی در برهمکنش گیاه-ویروس ایفا میکند که میتواند منجر به مقاومت گیاه یا بیماریزایی در گیاه میزبان شود. بنابراین، شناخت بیشتر سیستم یوبیکوئیتین پروتئازوم و بررسی نقش آن در برهمکنش ویروس-گیاه، می-تواند باعث توسعه روشهای جدید برای افزایش مقاومت به آلودگیهای ویروسی در گیاهان شود.
فهرست منابع
1. Alcaide-Loridan C, Jupin I (2012) Ubiquitin and plant viruses, let's play together. Plant Physiology 160:72-82. [DOI:10.1104/pp.112.201905] [PMID] [PMCID]
2. Barajas D, Jiang Y, Nagy PD (2009) A unique role for the host ESCRT proteins in replication of Tomato bushy stunt virus. PLoS Pathogens 5:e1000705. [DOI:10.1371/journal.ppat.1000705] [PMID] [PMCID]
3. Baumberger N, Tsai CH, Lie M, Havecker E, Baulcombe DC (2007) The Polerovirus silencing suppressor P0 targets argonaute proteins for degradation. Current Biology 17:1609-1614. [DOI:10.1016/j.cub.2007.08.039] [PMID]
4. Camborde L, Planchais S, Tournier V, Jakubiec A, Drugeon G, Lacassagne E, Pflieger S, Chenon M, Jupin I (2010) The ubiquitin-proteasome system regulates the accumulation of Turnip yellow mosaic virus RNA-dependent RNA polymerase during viral infection. The Plant Cell 22:3142-3152. [DOI:10.1105/tpc.109.072090] [PMID] [PMCID]
5. Chen B, Lin L, Lu Y, Peng J, Zheng H, Yang Q, Rao S, Wu G, Li J, Chen Z, Song B (2020) Ubiquitin-Like protein 5 interacts with the silencing suppressor p3 of rice stripe virus and mediates its degradation through the 26S proteasome pathway. PLoS Pathogens 16:e1008780. [DOI:10.1371/journal.ppat.1008780] [PMID] [PMCID]
6. Chen IH, Chang JE, Wu CY, Huang YP, Hsu YH, Tsai CH (2019) An E3 ubiquitin ligase from Nicotiana benthamiana targets the replicase of Bamboo mosaic virus and restricts its replication. Molecular Plant Pathology 20:673-684. [DOI:10.1111/mpp.12784] [PMID] [PMCID]
7. Chen L, Cheng C, Zhang C, Yao Q, Zhao E (2013) Ubiquitin-conjugating enzyme involved in the immune response caused by pathogens invasion. Open Journal of Immunology 3:93-97. [DOI:10.4236/oji.2013.33013]
8. Chenon M, Camborde L, Cheminant S, Jupin I (2012) A viral deubiquitylating enzyme targets viral RNA-dependent RNA polymerase and affects viral infectivity. The EMBO Journal 31:741-753. [DOI:10.1038/emboj.2011.424] [PMID] [PMCID]
9. Dielen AS, Sassaki FT, Walter J, Michon T, Menard G, Pagny G, Krause-Sakate R, Maia IDG, Badaoui S, Le Gall O, Candresse T (2011) The 20S proteasome alpha(5) subunit of Arabidopsis thaliana carries an RNase activity and interacts in planta with the lettuce mosaic potyvirus HcPro protein. Molecular Plant Pathology 12:137-150. [DOI:10.1111/j.1364-3703.2010.00654.x] [PMID] [PMCID]
10. Eini O, Dogra S, Selth LA, Dry IB, Randles JW, Rezaian MA (2009) Interaction with a host ubiquitin-conjugating enzyme is required for the pathogenicity of a geminiviral DNA beta satellite. Molecular Plant-Microbe Interactions 22:737-746. [DOI:10.1094/MPMI-22-6-0737] [PMID]
11. Gancarz BL, Hao L, He Q, Newton MA, Ahlquist P (2011) Systematic identification of novel, essential host genes affecting bromovirus RNA replication. PLoS One 6:e23988. [DOI:10.1371/journal.pone.0023988] [PMID] [PMCID]
12. Garcia‐Ruiz H (2019) Host factors against plant viruses. Molecular Plant Pathology 20:1588-1601. [DOI:10.1111/mpp.12851] [PMID] [PMCID]
13. Glickman MH, Ciechanover A (2002) The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiological Reviews 82:373-428. [DOI:10.1152/physrev.00027.2001] [PMID]
14. Ikeda F, Dikic I (2008) A typical ubiquitin chains: new molecular signals. Protein Modifications: Beyond the Usual Suspects' review series. EMBO Reports 9:536-542. [DOI:10.1038/embor.2008.93] [PMID] [PMCID]
15. Jia Q, Liu N, Xie K, Dai Y, Han S, Zhao X, Qian L, Wang Y, Zhao J, Gorovits R, Xie D (2016) CLCuMuB βC1 subverts ubiquitination by interacting with NbSKP1s to enhance geminivirus infection in Nicotiana benthamiana. PLoS Pathogens 12(6):1005668. [DOI:10.1371/journal.ppat.1005668] [PMID] [PMCID]
16. Jockusch H, Wiegand C (2003) Misfolded plant virus proteins: Elicitors and targets of ubiquitylation. FEBS Letters 545:229-232. [DOI:10.1016/S0014-5793(03)00549-0]
17. Johnson ES (2002) Ubiquitin branches out. Nature Cell Biology 4:295-298. [DOI:10.1038/ncb1202-e295] [PMID]
18. Ju HJ, Ye CM, Verchot-Lubicz J (2008) Mutational analysis of PVX TGBp3 links subcellular accumulation and protein turnover. Virology 375:103-117. [DOI:10.1016/j.virol.2008.01.030] [PMID]
19. Kelley DR, Estelle M (2012) Ubiquitin-mediated control of plant hormone signaling. Plant Physiology 160:47-55. [DOI:10.1104/pp.112.200527] [PMID] [PMCID]
20. Lageix S, Catrice O, Deragon JM, Gronenborn B, Pélissier T, Ramírez BC (2007) The nanovirus-encoded Clink protein affects plant cell cycle regulation through interaction with the retinoblastoma-related protein. Journal of Virology 81:4177-4185. [DOI:10.1128/JVI.02103-06] [PMID] [PMCID]
21. Lai J, Chen H, Teng K, Zhao Q, Zhang Z, Li Y, Liang L, Xia R, Wu Y, Guo H, Xie Q (2009) RKP, a RING finger E3 ligase induced by BSCTV C4 protein, affects geminivirus infection by regulation of the plant cell cycle. The Plant Journal 57:905-917. [DOI:10.1111/j.1365-313X.2008.03737.x] [PMID]
22. Lechner E, Achard P, Vansiri A, Potuschak T, Genschik P (2006) F-box proteins everywhere. Current Opinion in Plant Biology 9:631-638. [DOI:10.1016/j.pbi.2006.09.003] [PMID]
23. Lozano-Durán R, Rosas-Díaz T, Gusmaroli G, Luna AP, Taconnat L, Deng XW, Bejarano ER (2011) Geminiviruses subvert ubiquitination by altering CSN-mediated derubylation of SCF E3 ligase complexes and inhibit jasmonate signaling in Arabidopsis thaliana. The Plant Cell 23:1014-1032. [DOI:10.1105/tpc.110.080267] [PMID] [PMCID]
24. Martelli GP, Adams MJ, Kreuze JF, Dolja VV (2007) Family Flexiviridae: a case study in virion and genome plasticity. Annual Review of Phytopathology 45:73-100. [DOI:10.1146/annurev.phyto.45.062806.094401] [PMID]
25. Mazzucotelli E, Belloni S, Marone D, De Leonardis AM, Guerra D, Di Fonzo N, Cattivelli L, Mastrangelo AM (2006) The E3 ubiquitin ligase gene family in plants: regulation by degradation. Current Genomics 7:509-522. [DOI:10.2174/138920206779315728] [PMID] [PMCID]
26. Metzger MB, Hristova VA, Weissman AM (2012) HECT and ring finger families of e3 ubiquitin ligases at a glance. Journal of Cell Science 125:531-537. [DOI:10.1242/jcs.091777] [PMID] [PMCID]
27. Metzger MB, Pruneda JN, Klevit RE, Weissman AM (2014) RING-type E3 ligases: master manipulators of E2 ubiquitin-conjugating enzymes and ubiquitination. Biochimica et Biophysica Acta (BBA)-Molecular Cell Research 1843:47-60. [DOI:10.1016/j.bbamcr.2013.05.026] [PMID] [PMCID]
28. Pazhouhandeh M, Dieterle M, Marrocco K, Lechner E, Berry B, Brault V, Hemmer O, Kretsch, T, Richards KE, Genschik P, Ziegler-Graff V (2006) F-box-like domain in the polerovirus protein P0 is required for silencing suppressor function. Proceedings of the National Academy of Sciences of the United States of America 103:1994-1999. [DOI:10.1073/pnas.0510784103] [PMID] [PMCID]
29. Reichel C, Beachy RN (2000) Degradation of Tobacco mosaic virus movement protein by the 26s proteasome. Journal of Virology 74:3330-3337. [DOI:10.1128/JVI.74.7.3330-3337.2000] [PMID] [PMCID]
30. Ren H, Santner A, del Pozo JC, Murray JA, Estelle M (2008) Degradation of the cyclin-dependent kinase inhibitor KRP1 is regulated by two different ubiquitin E3 ligases. The Plant Journal 53:705-716. [DOI:10.1111/j.1365-313X.2007.03370.x] [PMID]
31. Sanchez-Durán MA, Dallas MB, Ascencio-Ibañez JT, Reyes MI, Arroyo-Mateos M, Ruiz-Albert J, Hanley-Bowdoin L, Bejarano ER (2011) Interaction between geminivirus replication protein and the SUMO-conjugating enzyme is required for viral infection. Journal of Virology 85:9789-9800. [DOI:10.1128/JVI.02566-10] [PMID] [PMCID]
32. Schwechheimer C, Isono E (2010) The COP9 signalosome and its role in plant development. European Journal of Cell Biology 89:157-162. [DOI:10.1016/j.ejcb.2009.11.021] [PMID]
33. Sharma B, Joshi D, Yadav PK, Gupta AK, Bhatt TK (2016) Role of ubiquitin-mediated degradation system in plant biology. Frontiers in Plant Science 7:806. [DOI:10.3389/fpls.2016.00806] [PMID] [PMCID]
34. Sorel M, Mooney B, de Marchi R, Graciet E (2018) Ubiquitin/Proteasome system in plant pathogen responses. Annual Plant Reviews Online 15:65-116. [DOI:10.1002/9781119312994.apr0665]
35. Takizawa M, Goto A, Watanabe Y (2005) The tobacco ubiquitin-activating enzymes NtE1A and NtE1B are induced by Tobacco mosaic virus, wounding and stress hormones. Molecules & Cells 19:228-231.
36. Thiel H, Hleibieh K, Gilmer D, Varrelmann M (2012) The P25 pathogenicity factor of BNYVV targets the sugar beet 26S proteasome involved in the induction of a hypersensitive resistance response via interaction with an F-box protein. Molecular Plant-Microbe Interactions 25:1058-1072. [DOI:10.1094/MPMI-03-12-0057-R] [PMID]
37. Ulrich HD (2009) The SUMO system: an overview. Methods in Molecular Biology 497:3-16. [DOI:10.1007/978-1-59745-566-4_1] [PMID]
38. Verchot J (2016) Plant virus infection and the ubiquitin proteasome machinery: arms race along the endoplasmic reticulum. Viruses 8:314. [DOI:10.3390/v8110314] [PMID] [PMCID]
39. Vierstra RD (2009) The ubiquitin-26S proteasome system at the nexus of plant biology. Nature Reviews Molecular Cell Biology 10:385-397. [DOI:10.1038/nrm2688] [PMID]
40. Wang Q, Tao T, Han Y, Chen X, Fan Z, Li D, Yu J, Han C (2013) Nonstructural protein p7-2 encoded by Rice black-streaked dwarf virus interacts with skp1, a core subunit of scf ubiquitin ligase. Virology Journal 10:1-12. [DOI:10.1186/1743-422X-10-325] [PMID] [PMCID]
41. Wu D, Qi T, Li WX, Tian H, Gao H, Wang J, Ge J, Yao R, Ren C, Wang XB, Liu Y (2017) Viral effector protein manipulates host hormone signaling to attract insect vectors. Cell Research 27:402-415. [DOI:10.1038/cr.2017.2] [PMID] [PMCID]
42. Xiong R, Wang A (2013) SCE1, the SUMO-conjugating enzyme in plants that interacts with NIb, the RNA-dependent RNA polymerase of Turnip mosaic virus, is required for viral infection. Journal of Virology 87:4704-4715. [DOI:10.1128/JVI.02828-12] [PMID] [PMCID]
43. Ye C, Dickman MB, Whitham SA, Payton M, Verchot J (2011) The unfolded protein response is triggered by a plant viral movement protein. Plant Physiology 156:741-755. [DOI:10.1104/pp.111.174110] [PMID] [PMCID]
44. Yuan X, Zhang S, Liu S, Yu M, Su H, Shu H, Li X (2013) Global analysis of ankyrin repeat domain C3HC4-type RING finger gene family in plants. PLoS One 8:e58003. [DOI:10.1371/journal.pone.0058003] [PMID] [PMCID]
45. Zhang Z, Chen H, Huang X, Xia R, Zhao Q, Lai J, Teng K, Li Y, Liang L, Du Q, Zhou X, Guo H, Xie Q (2011) BSCTV C2 attenuates the degradation of SAMDC1 to suppress DNA methylation-mediated gene silencing in Arabidopsis. The Plant Cell 23:273-288. [DOI:10.1105/tpc.110.081695] [PMID] [PMCID]
ارسال پیام به نویسنده مسئول
| بازنشر اطلاعات | |
 |
این مقاله تحت شرایط Creative Commons Attribution-NonCommercial 4.0 International License قابل بازنشر است. |
