Nup96 and HOS1 Are Mutually Stabilized and Gate CONSTANS Protein Level, Conferring Long-Day Photoperiodic Flowering Regulation in Arabidopsis

The nuclear pore complex profoundly affects the timing of flowering; however, the underlying mechanisms are poorly understood. Here, we report that ( ) acts as a negative regulator of long-day photoperiodic flowering in Arabidopsis ( ). Through multiple approaches, we identified the E3 ubiquitin lig...

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Published in:The Plant cell Vol. 32; no. 2; p. 374
Main Authors: Cheng, Zhiyuan, Zhang, Xiaomei, Huang, Penghui, Huang, Guowen, Zhu, Jinglong, Chen, Fulu, Miao, Yuchen, Liu, Liangyu, Fu, Yong-Fu, Wang, Xu
Format: Journal Article
Language:English
Published: England 01.02.2020
Subjects:
Arabidopsis - genetics
Arabidopsis - metabolism
Arabidopsis Proteins - genetics
Arabidopsis Proteins - metabolism
DNA-Binding Proteins - metabolism
Flowers - genetics
Flowers - metabolism
Gene Expression Regulation, Plant
Intracellular Signaling Peptides and Proteins - genetics
Intracellular Signaling Peptides and Proteins - metabolism
Mutation
Nuclear Envelope
Nuclear Pore Complex Proteins - genetics
Nuclear Pore Complex Proteins - metabolism
Nuclear Proteins - genetics
Nuclear Proteins - metabolism
Photoperiod
Transcription Factors - metabolism
Transcriptome
Ubiquitin-Protein Ligases
ISSN:1532-298X, 1532-298X
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Summary:The nuclear pore complex profoundly affects the timing of flowering; however, the underlying mechanisms are poorly understood. Here, we report that ( ) acts as a negative regulator of long-day photoperiodic flowering in Arabidopsis ( ). Through multiple approaches, we identified the E3 ubiquitin ligase HIGH EXPRESSION OF OSMOTICALLY RESPONSIVE GENE1 (HOS1) and demonstrated its interaction in vivo with Nup96. Nup96 and HOS1 mainly localize and interact on the nuclear membrane. Loss of function of leads to destruction of HOS1 proteins without a change in their mRNA abundance, which results in overaccumulation of the key activator of long-day photoperiodic flowering, CONSTANS (CO) proteins, as previously reported in mutants. Unexpectedly, mutation of strikingly diminishes Nup96 protein level, suggesting that Nup96 and HOS1 are mutually stabilized and thus form a novel repressive module that regulates CO protein turnover. Therefore, the and single and double mutants have highly similar early-flowering phenotypes and overlapping transcriptome changes. Together, this study reveals a repression mechanism in which the Nup96-HOS1 repressive module gates the level of CO proteins and thereby prevents precocious flowering in long-day conditions.
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ISSN:1532-298X
1532-298X
DOI:10.1105/tpc.19.00661