The transcription factor ZmNAC126 accelerates leaf senescence downstream of the ethylene signalling pathway in maize

2020 ◽  
Vol 43 (9) ◽  
pp. 2287-2300
Author(s):  
Zhen Yang ◽  
Chaoqi Wang ◽  
Kai Qiu ◽  
Huiru Chen ◽  
Zhongpeng Li ◽  
...  
2021 ◽  
Vol 8 (1) ◽  
Author(s):  
Kuo Yang ◽  
Jian-Ping An ◽  
Chong-Yang Li ◽  
Xue-Na Shen ◽  
Ya-Jing Liu ◽  
...  

AbstractJasmonic acid (JA) plays an important role in regulating leaf senescence. However, the molecular mechanisms of leaf senescence in apple (Malus domestica) remain elusive. In this study, we found that MdZAT10, a C2H2-type zinc finger transcription factor (TF) in apple, markedly accelerates leaf senescence and increases the expression of senescence-related genes. To explore how MdZAT10 promotes leaf senescence, we carried out liquid chromatography/mass spectrometry screening. We found that MdABI5 physically interacts with MdZAT10. MdABI5, an important positive regulator of leaf senescence, significantly accelerated leaf senescence in apple. MdZAT10 was found to enhance the transcriptional activity of MdABI5 for MdNYC1 and MdNYE1, thus accelerating leaf senescence. In addition, we found that MdZAT10 expression was induced by methyl jasmonate (MeJA), which accelerated JA-induced leaf senescence. We also found that the JA-responsive protein MdBT2 directly interacts with MdZAT10 and reduces its protein stability through ubiquitination and degradation, thereby delaying MdZAT10-mediated leaf senescence. Taken together, our results provide new insight into the mechanisms by which MdZAT10 positively regulates JA-induced leaf senescence in apple.


Planta ◽  
2017 ◽  
Vol 247 (1) ◽  
pp. 53-68 ◽  
Author(s):  
Tingting Ren ◽  
Jiawei Wang ◽  
Mingming Zhao ◽  
Xiaoming Gong ◽  
Shuxia Wang ◽  
...  

2016 ◽  
Vol 57 (5) ◽  
pp. 1098-1114 ◽  
Author(s):  
Maiana Reis Pimenta ◽  
Priscila Alves Silva ◽  
Giselle Camargo Mendes ◽  
Janaína Roberta Alves ◽  
Hanna Durso Neves Caetano ◽  
...  

2003 ◽  
Vol 119 (1) ◽  
pp. 90-99 ◽  
Author(s):  
Paola Maroni ◽  
Paola Bendinelli ◽  
Laura Tiberio ◽  
Francesca Rovetta ◽  
Roberta Piccoletti ◽  
...  

2011 ◽  
Vol 31 (4) ◽  
pp. 303-313 ◽  
Author(s):  
Xiang Zhou ◽  
Yanjuan Jiang ◽  
Diqiu Yu

2015 ◽  
Vol 71 (4) ◽  
pp. 844-853 ◽  
Author(s):  
Mads Beich-Frandsen ◽  
Eric Aragón ◽  
Marta Llimargas ◽  
Jordi Benach ◽  
Antoni Riera ◽  
...  

Gene-expression changes observed inDrosophilaembryos after inducing the transcription factor Tramtrack led to the identification of the protein Expansion. Expansion contains an N-terminal domain similar in sequence to the MH2 domain characteristic of Smad proteins, which are the central mediators of the effects of the TGF-β signalling pathway. Apart from Smads and Expansion, no other type of protein belonging to the known kingdoms of life contains MH2 domains. To compare the Expansion and Smad MH2 domains, the crystal structure of the Expansion domain was determined at 1.6 Å resolution, the first structure of a non-Smad MH2 domain to be characterized to date. The structure displays the main features of the canonical MH2 fold with two main differences: the addition of an α-helical region and the remodelling of a protein-interaction site that is conserved in the MH2 domain of Smads. Owing to these differences, to the new domain was referred to as Nα-MH2. Despite the presence of the Nα-MH2 domain, Expansion does not participate in TGF-β signalling; instead, it is required for other activities specific to the protostome phyla. Based on the structural similarities to the MH2 fold, it is proposed that the Nα-MH2 domain should be classified as a new member of the Smad/FHA superfamily.


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