Characterization of small ubiquitin-like modifier E3 ligase, OsSIZ1, mutant in rice
2012
Park, H.C., Gyeongsang National University, Jinju, Republic of Korea | Koo, S.C., Gyeongsang National University, Jinju, Republic of Korea | Kim, H., Gyeongsang National University, Jinju, Republic of Korea | Choi, W.K., Gyeongsang National University, Jinju, Republic of Korea | Yun, D.J., Gyeongsang National University, Jinju, Republic of Korea
Sumoylation is a reversible conjugation process that attaches the small ubiquitin modifier (SUMO) peptide to target proteins and regulates a wide variety of cellular functions in eucaryotes. As final step of the sumoylation, SUMO E3 ligases facilitate conjugation of SUMO to target proteins. To characterize the functions of the SUMO E3 ligases in Oryza sativa, we isolated a single recessive rice SUMO E3 ligase, Ossiz1-2 mutant. In addition, we also confirmed the interaction between OsSIZ1/-2 and OsSUMO1, respectively, by using an Agrobacterium-based tobacco luciferase transient expression system. Ossiz1-2 mutant exhibited approximately 20% reduction in growth and developmental units compared with wild type. Especially, number of filled seeds and total seed weight were dramatically decreased in the Ossiz1-2 mutant rice. Thus, these results suggest that sumoylation by the OsSIZ1 as SUMO E3 ligase plays an important role in regulating growth and development in rice.
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