The F-box protein SHORT PRIMARY ROOT modulates primary root meristem activity by targeting SEUSS-LIKE protein for degradation in rice

被引:2
|
作者
Ma, Nini [1 ]
Li, Nian [1 ]
Yu, Zhongmao [1 ]
Chen, Chunli [1 ]
Zhou, Dao-Xiu [1 ,2 ]
Zhao, Yu [1 ]
机构
[1] Huazhong Agr Univ, Natl Key Lab Crop Genet Improvement, Hubei Hongshan Lab, Wuhan 430070, Peoples R China
[2] Univ Paris Saclay, Inst Plant Sci Paris Saclay IPS2, CNRS, INRAE, F-91405 Orsay, France
基金
中国国家自然科学基金;
关键词
F-box protein; primary root development; rice; SLK (SEUSS-LIKE); ubiquitination; REGULATORY PROTEINS; SELECTIVE AUTOPHAGY; GENE-EXPRESSION; ARABIDOPSIS; COMPLEX; FAMILY; LEUNIG;
D O I
10.1111/jipb.13492
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Root meristem activity is essential for root morphogenesis and adaptation, but the molecular mechanism regulating root meristem activity is not fully understood. Here, we identify an F-box family E3 ubiquitin ligase named SHORT PRIMARY ROOT (SHPR) that regulates primary root (PR) meristem activity and cell proliferation in rice. SHPR loss-of-function mutations impair PR elongation in rice. SHPR is involved in the formation of an SCF complex with the Oryza sativa SKP1-like protein OSK1/20. We show that SHPR interacts with Oryza sativa SEUSS-LIKE (OsSLK) in the nucleus and is required for OsSLK polyubiquitination and degradation by the ubiquitin 26S-proteasome system (UPS). Transgenic plants overexpressing OsSLK display a shorter PR phenotype, which is similar to the SHPR loss-of-function mutants. Genetic analysis suggests that SHPR promotes PR elongation in an OsSLK-dependent manner. Collectively, our study establishes SHPR as an E3 ubiquitin ligase that targets OsSLK for degradation, and uncovers a protein ubiquitination pathway as a mechanism for modulating root meristem activity in rice.
引用
收藏
页码:1937 / 1949
页数:13
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