BBX

Last update 08 May 2025

Basic Info

Synonyms

BBX, BBX high mobility group box domain containing, Bobby sox homolog

+ [5]

Introduction

Transcription factor that is necessary for cell cycle progression from G1 to S phase.

100 Clinical Results associated with BBX

100 Translational Medicine associated with BBX

0 Patents (Medical) associated with BBX

150

Literatures (Medical) associated with BBX

01 Mar 2025·International Journal of Biological Macromolecules

Genome-wide identification and expression analysis of the BBX gene family in Lagerstroemia indica grown under light stress

Article

Author: Li, Yongxin ; Li, Lu ; Pi, Bing ; Li, Zhihui ; Zhang, Yi ; Chen, Yi ; Qiao, Zhongquan ; Deng, Fuyuan ; Lei, Yuxing ; Chen, Jianjun

B-box proteins (BBX) play pivotal roles in the regulation of numerous growth and developmental processes in plants, particularly the light-mediated biosynthesis of pigments. To elucidate the role of BBX transcription factors in the anthocyanin biosynthetic pathway of Lagerstroemia indica leaves, this study identified 41 BBX genes in the L. indica genome. Using bioinformatics approaches, we predicted their structural and functional characteristics and examined the variations in leaf coloration under varying durations of darkness and the expression profiles of BBX genes. The LiBBX genes were categorized into five distinct subfamilies through phylogenetic analysis, with substantial gene expansion due to segmental duplication events. Promoter analysis demonstrated that the BBX family possesses an abundance of light-responsive cis-elements. Using protein interaction prediction followed by qPCR analysis, we identified 17 interacting partners. Notably, the expression levels of the majority of BBX genes in L.indica 'Ebony Embers' were significantly downregulated in the darkness compared to those in the light. Correlation analyses indicated that the expression levels of most BBX genes were positively correlated with both anthocyanin and chlorophyll contents. Ultimately, we discovered a core BBX protein, LiBBX4, which can interact with LiHY5, LiHYH, and LiCOP1, and verified its involvement in regulating anthocyanin synthesis using VIGS. This study for the first time revealed novel insights into the molecular mechanisms underlying light-induced leaf color changes in L.indica, which could provide a fundamental framework for the genetic improvement of L.indica and enhance its commercial appeal.

01 Feb 2025·Plant Physiology and Biochemistry

Plant U-box E3 ligase PpPUB59 regulates anthocyanin accumulation by ubiquitinating PpBBX24 in ‘Zaosu’ pear and its red bud mutation

Article

Author: Liu, Xiaofeng ; Li, Shuran ; Ou, Chunqing ; Qi, Liyong ; Li, He ; Jiang, Shuling ; Wang, Fei ; Zhang, Yanjie

Ubiquitination is the specific modification of target proteins in cells by ubiquitin molecules, which is under the action of a series of special enzymes such as ubiquitin-activating enzymes, binding, and ligase enzymes. Ubiquitination plays an essential role in anthocyanin accumulation in plants. There are few studies on the coloring of pear peel by ubiquitin ligase E3. In this study, an E3 ubiquitin ligase protein PpPUB59 with seven WD40 repeats was cloned. And the function of PpPUB59 on the ubiquitination and protein stability of PpBBX24 and Ppbbx24-del, and the possible action mechanism in the anthocyanin accumulation of 'Red Zaosu' was studied. Our results showed that the WD40 repeats were verified to be the key domain interacting with the VP domain of BBX protein. PpPUB59 could degrade PpBBX24 in vitro by interacting with the VP domain but could not degrade the mutant PpBBX24-del without the VP domain. Dual luciferase assay showed that Ppbbx24-del could activate the PpCHS promoter, while PpPUB59 did not interfere with this activation; PpBBX24 could not activate the promotor of PpCHS but could suppress the activation of PpHY5; when the PpPUB59 was co-expressed with PpBBX24 and PpHY5, the activation roles of PpHY5 in the promotor of PpCHS was not recovered. BiFC and yeast two-hybrid experiments showed that PpPUB59 could also interact with PpHY5, which may make it ubiquitinated and degraded by 26S proteasome. In conclusion, PpPUB59 played an essential role in pear anthocyanin accumulation by ubiquitinating the associated transcription factors. These findings clarified the mutant mechanism of the 'Red Zaosu' pear at the post-translational modification level and enriched the regulation theory of the pear anthocyanin accumulation.

01 Dec 2024·Plant, Cell & Environment

The B‐box protein BBX13/COL15 suppresses photoperiodic flowering by attenuating the action of CONSTANS in Arabidopsis

Article

Author: Yadukrishnan, Premachandran ; Sasidharan, Anagha ; Rahul, Puthan Valappil ; Datta, Sourav

AbstractThe optimal timing of transition from vegetative to floral reproductive phase is critical for plant productivity and agricultural yields. Light plays a decisive role in regulating this transition. The B‐box (BBX) family of transcription factors regulates several light‐mediated developmental processes in plants, including flowering. Here, we identify a previously uncharacterized group II BBX family member, BBX13/COL15, as a negative regulator of flowering under long‐day conditions. BBX13 is primarily expressed in the leaf vasculature, buds, and flowers, showing a similar spatial expression pattern to the major flowering time regulators CO and FT. bbx13 mutants flower early, while BBX13‐overexpressors exhibit delayed flowering under long days. Genetic analyses showed that BBX13 acts upstream to CO and FT and negatively regulates their expression. BBX13 physically interacts with CO and inhibits the CO‐mediated transcriptional activation of FT. In addition, BBX13 directly binds to the CORE2 motif on the FT promoter, where CO also binds. Chromatin immunoprecipitation data indicates that BBX13 reduces the in vivo binding of CO on the FT promoter. Through luciferase assay, we found that BBX13 inhibits the CO‐mediated transcriptional activation of FT. Together, these findings suggest that BBX13/COL15 represses flowering in Arabidopsis by attenuating the binding of CO on the FT promoter.

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