Functional characterization of DiMMS21, a SUMO ligase from Desmodium intortum
Functional characterization of DiMMS21, a SUMO ligase from Desmodium intortum
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DiMMS21(一种来自金钱草的 SUMO 连接酶)的功能表征
DOI:
10.1016/j.plaphy.2019.06.003
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发表时间:
2019
影响因子:
6.5
通讯作者:
Lai Jianbin
中科院分区:
文献类型:
--
作者:
Zhou Xuan;Du Jinju;Liu Yiyang;Yang Chengwei;Lai Jianbin
SUMOylation is an important protein modification that regulates the properties of substrate proteins in a variety of cellular processes. SUMOylation is catalyzed via a cascade of enzymes and is usually stimulated by SUMO E3 ligases. However, the molecular functions and regulatory mechanisms of SUMOylation in forage crops are unknown. Here, we isolated and functionally characterized DiMMS21, a homolog of theArabidopsis thalianaSUMO ligase AtMMS21, from the forage legumeDesmodium intortum.DiMMS21is expressed ubiquitously in variousD. intortumorgans and its encoded protein is found in the cytoplasm and nucleus. Bioinformatics analysis indicated that DiMMS21 contains a conserved SP-RING domain that is required for its activity. Biochemical evidence supports the notion that this protein is a functional SUMO ligase. When expressed in anArabidopsis mms21mutant,DiMMS21completely rescued the defects in root, leaf, and silique development. The results from cotyledon greening and marker gene expression suggested thatDiMMS21can only partially complements the role of AtMMS21 in abscisic acid (ABA) responses. In summary, we characterized the molecular features of DiMMS21 and uncovered potential roles of this SUMO ligase in development and ABA responses, increasing our understanding on the function of SUMOylation in forage crops.