A potential role of UBC28 interacting RING finger protein TaRF1 in spike development of wheat

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• 作者：Min Jeong Hong ; Yong Weon Seo
• 关键词：Wheat ; RING finger protein ; TaRF1 ; TaUBC28 ; Spike development
• 刊名：Journal of Plant Biochemistry and Biotechnology
• 出版年：2014
• 出版时间：October 2014
• 年：2014
• 卷：23
• 期：4
• 页码：421-429
• 全文大小：2,422 KB
• 参考文献：1. Abramoff MD, Magelhaes PJ, Ram SJ (2004) Image processing with ImageJ. Biophoton Int 11:36-2
  2. Barlow P, Luisi B, Milner A, Elliott M, Everett R (1994) Structure of the C3HC4 domain by 1H-nuclear magnetic resonance spectroscopy. A new structural class of zinc-finger. J Mol Biol 237:201-11 CrossRef
  3. Borden KLB, Freemont PS (1996) The RING finger domain: a recent example of a sequence—structure family. Curr Opin Struct Biol 6:395-01 CrossRef
  4. Chen H, Nelson R, Sherwood J (1994) Enhanced recovery of transformants of Agrobacterium tumefaciens after freeze-thaw transformation and drug selection. Biotechniques 16:664-68
  5. Chen D, Molitor A, Liu C, Shen WH (2010) The Arabidopsis PRC1-like ring-finger proteins are necessary for repression of embryonic traits during vegetative growth. Cell Res 20:1332-344 CrossRef
  6. Dasgupta A, Ramsey KL, Smith JS, Auble DT (2004) Sir Antagonist 1 (San1) is a ubiquitin ligase. J Biol Chem 279:26830-6838 CrossRef
  7. Deshaies RJ, Joazeiro CAP (2009) RING domain E3 ubiquitin ligases. Annu Rev Biochem 78:399-34 CrossRef
  8. Dong CH, Agarwal M, Zhang Y, Xie Q, Zhu JK (2006) The negative regulator of plant cold responses, HOS1, is a RING E3 ligase that mediates the ubiquitination and degradation of ICE1. Proc Natl Acad Sci USA 103:8281-286 CrossRef
  9. Glickman MH, Ciechanover A (2002) The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol Rev 82:373-28
  10. Guerra DD, Callis J (2012) Ubiquitin on the move: the ubiquitin modification system plays diverse roles in the regulation of endoplasmic reticulum-and plasma membrane-localized proteins. Plant Physiol 160:56-4 CrossRef
  11. Hardtke CS, Okamoto H, Stoop–Myer C, Deng XW (2002) Biochemical evidence for ubiquitin ligase activity of the Arabidopsis COP1 interacting protein 8 (CIP8). Plant J 30:385-94 CrossRef
  12. Hellmann H, Estelle M (2002) Plant development: regulation by protein degradation. Science 297:793-97 CrossRef
  13. Hong MJ, Kim DY, Kang SY, Kim DS, Kim JB, Seo YW (2012) Wheat F-box protein recruits proteins and regulates their abundance during wheat spike development. Mol Biol Rep 39:9681-696 CrossRef
  14. Hua Z, Vierstra RD (2011) The cullin-RING ubiquitin-protein ligases. Annu Rev Plant Biol 62:299-34 CrossRef
  15. Imai J, Maruya M, Yashiroda H, Yahara I, Tanaka K (2003) The molecular chaperone Hsp90 plays a role in the assembly and maintenance of the 26S proteasome. EMBO J 22:3557-567 CrossRef
  16. Kraft E, Stone SL, Ma L, Su N, Gao Y, Lau OS, Deng XW, Callis J (2005) Genome analysis and functional characterization of the E2 and RING-type E3 ligase ubiquitination enzymes of Arabidopsis. Plant Physiol 139:1597-611 CrossRef
  17. Lee HK, Cho SK, Son O, Xu Z, Hwang I, Kim WT (2009) Drought stress-induced Rma1H1, a RING membrane-anchor E3 ubiquitin ligase homolog, regulates aquaporin levels via ubiquitination in transgenic Arabidopsis plants. Plant Cell 21:622-41 CrossRef
  18. Lorick KL, Jensen JP, Fang S, Ong AM, Hatakeyama S, Weissman AM (1999) RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination. Proc Natl Acad Sci USA 96:11364-1369 CrossRef
  19. Mabb AM, Ehlers MD (2010) Ubiquitination in postsynaptic function and plasticity. Annu Rev Cell Dev Biol 26:179-10 CrossRef
  20. Nakamura N (2011) The role of the transmembrane RING finger proteins in cellular and organelle function. Membranes 1:354-93 CrossRef
  21. Pratt WB, Krishna P, Olsen LJ (2001) Hsp90-binding immunophilins in plants: the protein movers. Trends Plant Sci 6:54-8 CrossRef
  22. Qin R, Gao S, McDonald JA, Ajwa H, Shem-Tov S, Sullivan DA (2008) Effect of plastic tarps over raised-beds and potassium thiosulfate in furrows on chloropicrin emissions from drip fumigated fields. Chemosphere 72:558-63 CrossRef
  23. Richter K, Buchner J (2001) Hsp90: chaperoning signal transduction. J Cell Physiol 188:281-90 CrossRef
  24. Song XJ, Huang W, Shi M, Zhu MZ, Lin HX (2007) A QTL for rice grain width and weight encodes a previously unknown RING-type E3 ubiquitin ligase. Nat Genet 39:623-30 CrossRef
  25. Sonoda Y, Yao SG, Sako K, Sato T, Kato W, Ohto M, Ichikawa T, Matsui M, Yamaguchi J, Ikeda A (2007) SHA1, a novel RING finger protein, functions in shoot apical meristem maintenance in Arabidopsis. Plant J 50:586-96 CrossRef
  26. Stone SL, Hauksdóttir H, Troy A, Herschleb J, Kraft E, Callis J (2005) Functional analysis of the RING-type ubiquitin ligase family of Arabidopsis. Plant Physiol 137:13-0 CrossRef
  27. VanDemark AP, Hill CP (2002) Structural basis of ubiquitylation. Curr Opin Struct Biol 12:822-30 CrossRef
  28. Walter M, Chaban C, Schütze K, Batistic O, Weckermann K, N?ke C, Blazevic D, Grefen C, Schumacher K, Oecking C (2004) Visualization of protein interactions in living plant cells using bimolecular fluorescence complementation. Plant J 40:428-38 CrossRef
  29. Wang F, Deng XW (2011) Plant ubiquitin-proteasome pathway and its role in gibberellin signaling. Cell Res 21:1286-294 CrossRef
  30. Wang W, Vinocur B, Shoseyov O, Altman A (2004) Role of plant heat-shock proteins and molecular chaperones in the abiotic stress response. Trends Plant Sci 9:244-52 CrossRef
  31. Wen R, Newton L, Li G, Wang H, Xiao W (2006) Arabidopsis thaliana UBC13: implication of error-free DNA damage tolerance and Lys63-linked polyubiquitylation in plants. Plant Mol Biol 61:241-53 CrossRef
  32. Wydro M, Kozubek E, Lehmann P (2006) Optimization of transient Agrobacterium-mediated gene expression system in leaves of Nicotiana benthamiana. Acta Biochim Pol 53:289-98
  33. Xie Q, Guo HS, Dallman G, Fang S, Weissman AM, Chua NH (2002) SINAT5 promotes ubiquitin-related degradation of NAC1 to attenuate auxin signals. Nature 419:167-70 CrossRef
  34. Xu R, Quinn Li Q (2003) A RING-H2 zinc-finger protein gene RIE1 is essential for seed development in Arabidopsis. Plant Mol Biol 53:37-0 CrossRef
  35. Young JC, Moarefi I, Hartl FU (2001) Hsp90: a specialized but essential protein-folding tool. J Cell Biol 154:267-73 CrossRef
  36. Yu Y, Xu W, Wang S, Xu Y, Li H, Wang Y, Li S (2011) VpRFP1, a novel C4C4-type RING finger protein gene from Chinese wild Vitispseudoreticulata, functions as a transcriptional activator in defence response of grapevine. J Exp Bot 62:5671-682 CrossRef
  37. Zhang Y (2003) Transcriptional regulation by histone ubiquitination and deubiquitination. Genes Dev 17:2733-740 CrossRef
  38. Zhang X, Garreton V, Chua NH (2005) The AIP2 E3 ligase acts as a novel negative regulator of ABA signaling by promoting ABI3 degradation. Genes Dev 19:1532-543 CrossRef
  
• 作者单位：Min Jeong Hong (1) (2)
  Yong Weon Seo (1)
  
  1. Division of Biotechnology, Korea University, Anam-Dong, Seongbuk-Gu, Seoul, 136-701, Republic of Korea
  2. Advanced Radiation Technology Institute, Korea Atomic Energy Research Institute, 1266 Sinjeong, Jeongeup, Jeonbuk, 580-185, Republic of Korea
  
• ISSN：0974-1275

文摘

RING finger proteins are the most abundant proteins in plants and may be essential for diverse aspects of cellular regulation in plant growth and development. Many RING finger proteins are E3 ubiquitin ligases, which play important roles in protein-protein interactions and ubiquitin-dependent protein degradation. The TaRF1 gene encodes a novel RING finger protein. In this study, we characterized the wheat (Triticum aestivum) RING finger domain as a hexapoid wheat ubiquitin ligase. To study the role of TaRF1 in wheat, we isolated TaRF1 from wheat spike cDNA. TaRF1 was 756?bp and encoded a putative 251-amino-acid with a predicted molecular mass of 28.57?kDa and isoelectric point of 5.75. A typical C3HC4-type RING finger domain was found at the C-terminal region of the TaRF1 protein. TaRF1 expression was investigated in the developmental stages and under various stresses by using reverse transcription polymerase chain reaction and was confirmed by subcellular localization of TaRF1 labeled with green fluorescent protein. Using the yeast 2-hybrid screen, we identified potential TaRF1-interacting proteins in a wheat spike library. Among the 8 clones that were identified as potential interacting partners of TaRF1 using yeast 2-hybrid screening, we found the strongest interaction between TaRF1 and the ubiquitin E2 enzyme TaUBC28 in tobacco leaves through biomolecular fluorescence complementation. The selectivity of interactions between E2 enzymes and RING E3 ligases represents a central and crucial part of the ubiquitin-conjugation pathways in organisms. These results indicate that the TaRF1 protein can interact with TaUBC28 in vitro and in vivo.