OsRFPH2-10, a RING-H2 finger E3 ubiquitin ligase, is involved in rice antiviral defense in the early stages of rice dwarf virus infection

Molecular Plant

Volumn 7, Issue 6, 2014, Pages 1058-1060

  Liu, Lifang ^a   Jin, Lian ^a   Huang, Xiahe ^b   Geng, Yongtao ^a   Li, Feng ^a   Qin, Qingqing ^a   Wang, Rui ^a   Ji, Shaoyi ^a   Zhao, Shanshan ^a   Xie, Qi ^b   Wei, Chunhong ^a   Xie, Can ^a   Ding, Biao ^c   Li, Yi ^a  

^a PEKING UNIVERSITY   (China)

^b INSTITUTE OF GENETICS AND DEVELOPMENTAL BIOLOGY   (China)

^c OHIO STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN BINDING; UBIQUITIN PROTEIN LIGASE; VEGETABLE PROTEIN;

ENZYMOLOGY; GENETICS; METABOLISM; RICE; VIROLOGY;

ORYZA SATIVA; PLANT PROTEINS; PROTEIN BINDING; UBIQUITIN-PROTEIN LIGASES;

EID: 84901932222     PISSN: 16742052     EISSN: 17529867     Source Type: Journal    
DOI: 10.1093/mp/ssu007     Document Type: Letter

References (10)

1. Alcaide-Loridan, C., and Jupin, I. (2012). Ubiquitin and plant viruses, let's play together! Plant Physiol. 160, 72-82
2. Chen, L., and Hellmann, H. (2013). Plant E3 ligases: flexible enzymes in a sessile world. Mol. Plant. 6, 1388-1404
3. Dreher, K., and Callis, J. (2007). Ubiquitin, hormones and biotic stress in plants. Ann. Bot. 99, 787-822 (Pubitemid 47355841)
4. Freemont, P.S. (2000). Ubiquitination: RING for destruction? Curr. Biol. 10, R84-R87 (Pubitemid 30079189)
5. Jackson, P.K., Eldridge, A.G., Freed, E., Furstenthal, L., Hsu, J.Y., Kaiser, B.K., and Reimann, J.D.R. (2000). The lore of the RINGs: substrate recognition and catalysis by ubiquitin ligases. Trends Cell Biol. 10, 429-439
6. Lim, S.D., Hwang, J.G., Jung, C.G., Hwang, S.G., Moon, J.C., and Jang, C.S. (2013). Comprehensive analysis of the rice RING E3 ligase family reveals their functional diversity in response to abiotic stress. DNA Res. 20, 299-314
7. Omura, T., Yan, J., Zhong, B., Wada, M., Zhu, Y., Tomaru, M., Maruyama, W., Kikuchi, A., Watanabe, Y., Kimura, I., et al. (1998). The P2 protein of rice dwarf phytoreovirus is required for adsorption of the virus to cells of the insect vector. J. Virol. 72, 9370-9373 (Pubitemid 28471890)
8. Pu, Y., Kikuchi, A., Moriyasu, Y., Tomaru, M., Jin, Y., Suga, H., Hagiwara, K., Akita, F., Shimizu, T., Netsu, O., et al. (2011). Rice dwarf viruses with dysfunctional genomes generated in plants are filtered out in vector insects: implications for the origin of the virus. J. Virol. 85, 2975-2979
9. Zhou, F., Pu, Y., Wei, T., Liu, H., Deng, W., Wei, C., Ding, B., Omura, T., and Li, Y. (2007). The P2 capsid protein of the nonenveloped rice dwarf phytoreovirus induces membrane fusion in insect host cells. Proc. Natl Acad. Sci. U S A. 104, 19547-19552
10. Zhu, S., Gao, F., Cao, X., Chen, M., Ye, G., Wei, C., and Li, Y. (2005). The rice dwarf virus P2 protein interacts with ent-kaurene oxidases in vivo, leading to reduced biosynthesis of gibberellins and rice dwarf symptoms. Plant Physiol. 139, 1935-1945. (Pubitemid 43899829)