Two bHLH Transcription Factors, bHLH48 and bHLH60, Associate with PHYTOCHROME INTERACTING FACTOR 7 to Regulate Hypocotyl Elongation in Arabidopsis Thaliana

2020 ◽  
Author(s):  
Chuanwei Yang ◽  
Sha Huang ◽  
Yue Zeng ◽  
Chang Liu ◽  
Qinyi Ma ◽  
...  
2016 ◽  
Vol 170 (4) ◽  
pp. 2478-2493 ◽  
Author(s):  
Xiaoli Li ◽  
Huimin Zhang ◽  
Qin Ai ◽  
Gang Liang ◽  
Diqiu Yu

2020 ◽  
Vol 11 ◽  
Author(s):  
Maurizio Di Marzo ◽  
Irma Roig-Villanova ◽  
Eva Zanchetti ◽  
Francesca Caselli ◽  
Veronica Gregis ◽  
...  

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Gilor Kelly ◽  
Danja Brandsma ◽  
Aiman Egbaria ◽  
Ofer Stein ◽  
Adi Doron-Faigenboim ◽  
...  

AbstractThe hypocotyls of germinating seedlings elongate in a search for light to enable autotrophic sugar production. Upon exposure to light, photoreceptors that are activated by blue and red light halt elongation by preventing the degradation of the hypocotyl-elongation inhibitor HY5 and by inhibiting the activity of the elongation-promoting transcription factors PIFs. The question of how sugar affects hypocotyl elongation and which cell types stimulate and stop that elongation remains unresolved. We found that overexpression of a sugar sensor, Arabidopsis hexokinase 1 (HXK1), in guard cells promotes hypocotyl elongation under white and blue light through PIF4. Furthermore, expression of PIF4 in guard cells is sufficient to promote hypocotyl elongation in the light, while expression of HY5 in guard cells is sufficient to inhibit the elongation of the hy5 mutant and the elongation stimulated by HXK1. HY5 exits the guard cells and inhibits hypocotyl elongation, but is degraded in the dark. We also show that the inhibition of hypocotyl elongation by guard cells’ HY5 involves auto-activation of HY5 expression in other tissues. It appears that guard cells are capable of coordinating hypocotyl elongation and that sugar and HXK1 have the opposite effect of light on hypocotyl elongation, converging at PIF4.


2007 ◽  
Vol 47 (supplement) ◽  
pp. S54
Author(s):  
Koji HASEGAWA ◽  
Tatsushi GOTO ◽  
Daisuke KITANO ◽  
Mari KOTOURA ◽  
Fumio TOKUNAGA ◽  
...  

2021 ◽  
Vol 118 (39) ◽  
pp. e2109063118
Author(s):  
Yang Li ◽  
Cheng Kai Lu ◽  
Chen Yang Li ◽  
Ri Hua Lei ◽  
Meng Na Pu ◽  
...  

IRON MAN (IMA) peptides, a family of small peptides, control iron (Fe) transport in plants, but their roles in Fe signaling remain unclear. BRUTUS (BTS) is a potential Fe sensor that negatively regulates Fe homeostasis by promoting the ubiquitin-mediated degradation of bHLH105 and bHLH115, two positive regulators of the Fe deficiency response. Here, we show that IMA peptides interact with BTS. The C-terminal parts of IMA peptides contain a conserved BTS interaction domain (BID) that is responsible for their interaction with the C terminus of BTS. Arabidopsis thaliana plants constitutively expressing IMA genes phenocopy the bts-2 mutant. Moreover, IMA peptides are ubiquitinated and degraded by BTS. bHLH105 and bHLH115 also share a BID, which accounts for their interaction with BTS. IMA peptides compete with bHLH105/bHLH115 for interaction with BTS, thereby inhibiting the degradation of these transcription factors by BTS. Genetic analyses suggest that bHLH105/bHLH115 and IMA3 have additive roles and function downstream of BTS. Moreover, the transcription of both BTS and IMA3 is activated directly by bHLH105 and bHLH115 under Fe-deficient conditions. Our findings provide a conceptual framework for understanding the regulation of Fe homeostasis: IMA peptides protect bHLH105/bHLH115 from degradation by sequestering BTS, thereby activating the Fe deficiency response.


2017 ◽  
Vol 10 (11) ◽  
pp. 1461-1464 ◽  
Author(s):  
Houping Wang ◽  
Yang Li ◽  
Jinjing Pan ◽  
Dengji Lou ◽  
Yanru Hu ◽  
...  

Biology Open ◽  
2021 ◽  
Author(s):  
Konstantina Filippopoulou ◽  
Carole Couillault ◽  
Vincent Bertrand

Neural bHLH transcription factors play a key role in the early steps of neuronal specification in many animals. We have previously observed that the Achaete-Scute HLH-3, the Olig HLH-16 and their binding partner the E protein HLH-2 activate the terminal differentiation program of a specific class of cholinergic neurons, AIY, in C. elegans. Here we identify a role for a fourth bHLH, the Neurogenin NGN-1, in this process, raising the question of why so many neural bHLHs are required for a single neuronal specification event. Using quantitative imaging we show that the combined action of different bHLHs is needed to activate the correct level of expression of the terminal selector transcription factors TTX-3 and CEH-10 that subsequently initiate and maintain the expression of a large battery of terminal differentiation genes. Surprisingly, the different bHLHs have an antagonistic effect on another target, the proapoptotic BH3-only factor EGL-1, normally not expressed in AIY and otherwise detrimental for its specification. We propose that the use of multiple neural bHLHs allows robust neuronal specification while, at the same time, preventing spurious activation of deleterious genes.


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