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벼의 small ubiquitin-like modifier E3 ligase, OsSIZ1 돌연변이체의 특성 분석

Characterization of small ubiquitin-like modifier E3 ligase, OsSIZ1, mutant in rice

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초록

식물체에서 sumoylation 기작은 성장 및 발달에 중요한 기능을 수행할 것이다. 특히, SUMO E3 ligase는 SUMO 단백질을 목적 단백질로 전달해주는 마지막 단계의 sumoylation 기작 구성요소이며, 다양한 신호전달에 특이성을 나타내는 것으로 보고되고 있다. 본 연구에서는 벼에서 SUMO E3ligase, SIZ1 유전자에 T-DNA가 삽입된 Ossiz1-2 돌연변이 식물체를 분석하였다. 그리고, OsSIZ1 단백질이 OsSUMO1 단백질과 상호작용함으로써 OsSIZ1이 SUMO E3 ligase의 기능을 수행할 것으로 예측하였다. Ossiz1-2 돌연변이 식물체는 형태학적으로 발달과 성장의 다양한 부분에서 미성숙상태로 유지됨이 보였다. 특히, 야생형인 동진벼와 비교하여 초장의 성장 및 등숙율에서 상당히 낮은 정도를보여 주었다. 이와 같이, 벼에서 SUMO E3 ligase로써OsSIZ1 단백질의 생리학적인 기능은 성장과 발달 그리고, 수확량에 관여하는 단백질을 sumoylation 시키는 기작에서 역할을 수행할 것으로 사려된다.

Abstract

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 E3ligases 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 E3ligase plays an import

참고문헌 (39)

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