Diversification of SQUAMOSA promoter binding protein-like (SPL) genes by changes of miR156/529 binding sites in land plants

Plant Gene ◽  
2018 ◽  
Vol 14 ◽  
pp. 55-63
Author(s):  
Shu-Dong Zhang ◽  
Li-Zhen Ling
Keyword(s):  
Binding Sites ◽  
Binding Protein ◽  
Land Plants ◽  
Squamosa Promoter Binding Protein ◽  
Spl Genes

scholarly journals Roles of the GA-mediated SPL Gene Family and miR156 in the Floral Development of Chinese Chestnut (Castanea mollissima)

2019 ◽  
Vol 20 (7) ◽  
pp. 1577 ◽  
Author(s):  
Guosong Chen ◽  
Jingtong Li ◽  
Yang Liu ◽  
Qing Zhang ◽  
Yuerong Gao ◽  
...  
Keyword(s):  
Target Genes ◽  
Floral Development ◽  
Binding Protein ◽  
Expression Patterns ◽  
Evolutionary Relationship ◽  
Deciduous Tree ◽  
Main Function ◽  
Squamosa Promoter Binding Protein ◽  
Spl Genes ◽  
Castanea Mollissima

Chestnut (Castanea mollissima) is a deciduous tree species with major economic and ecological value that is widely used in the study of floral development in woody plants due its monoecious and out-of-proportion characteristics. Squamosa promoter-binding protein-like (SPL) is a plant-specific transcription factor that plays an important role in floral development. In this study, a total of 18 SPL genes were identified in the chestnut genome, of which 10 SPL genes have complementary regions of CmmiR156. An analysis of the phylogenetic tree of the squamosa promoter-binding protein (SBP) domains of the SPL genes of Arabidopsis thaliana, Populus trichocarpa, and C. mollissima divided these SPL genes into eight groups. The evolutionary relationship between poplar and chestnut in the same group was similar. A structural analysis of the protein-coding regions (CDSs) showed that the domains have the main function of SBP domains and that other domains also play an important role in determining gene function. The expression patterns of CmmiR156 and CmSPLs in different floral organs of chestnut were analyzed by real-time quantitative PCR. Some CmSPLs with similar structural patterns showed similar expression patterns, indicating that the gene structures determine the synergy of the gene functions. The application of gibberellin (GA) and its inhibitor (Paclobutrazol, PP333) to chestnut trees revealed that these exert a significant effect on the number and length of the male and female chestnut flowers. GA treatment significantly increased CmmiR156 expression and thus significantly decreased the expression of its target gene, CmSPL6/CmSPL9/CmSPL16, during floral bud development. This finding indicates that GA might indirectly affect the expression of some of the SPL target genes through miR156. In addition, RNA ligase-mediated rapid amplification of the 5′ cDNA ends (RLM-RACE) experiments revealed that CmmiR156 cleaves CmSPL9 and CmSPL16 at the 10th and 12th bases of the complementary region. These results laid an important foundation for further study of the biological function of CmSPLs in the floral development of C. mollissima.

scholarly journals Molecular Cloning and Characterization of SQUAMOSA-Promoter Binding Protein-Like Gene FvSPL10 from Woodland Strawberry (Fragaria vesca)

Plants ◽  
2019 ◽  
Vol 8 (9) ◽  
pp. 342 ◽  
Author(s):  
Jinsong Xiong ◽  
Yibo Bai ◽  
Chuangju Ma ◽  
Hongyu Zhu ◽  
Dan Zheng ◽  
...  
Keyword(s):  
Plant Growth ◽  
Growth And Development ◽  
Binding Protein ◽  
Ectopic Expression ◽  
Plant Growth And Development ◽  
Woodland Strawberry ◽  
Squamosa Promoter Binding Protein ◽  
Spl Genes

SQUAMOSA-promoter binding protein-like (SPL) proteins are plant-specific transcript factors that play essential roles in plant growth and development. Although many SPL genes have been well characterized in model plants like Arabidopsis, rice and tomato, the functions of SPLs in strawberry are still largely elusive. In the present study, we cloned and characterized FvSPL10, the ortholog of AtSPL9, from woodland strawberry. Subcellular localization shows FvSPL10 localizes in the cell nucleus. The luciferase system assay indicates FvSPL10 is a transcriptional activator, and both in vitro and in vivo assays indicate FvSPL10 could bind to the promoter of FvAP1 and activate its expression. Ectopic expression of FvSPL10 in Arabidopsis promotes early flowering and increases organs size. These results demonstrate the multiple regulatory roles of FvSPL10 in plant growth and development and lay a foundation for investigating the biological functions of FvSPL10 in strawberry.

scholarly journals Developmental Functions of miR156-Regulated SQUAMOSA PROMOTER BINDING PROTEIN-LIKE (SPL) Genes in Arabidopsis thaliana

PLoS Genetics ◽  
2016 ◽  
Vol 12 (8) ◽  
pp. e1006263 ◽  
Author(s):  
Mingli Xu ◽  
Tieqiang Hu ◽  
Jianfei Zhao ◽  
Mee-Yeon Park ◽  
Keith W. Earley ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Binding Protein ◽  
Squamosa Promoter Binding Protein ◽  
Spl Genes

scholarly journals Genome-Wide Analysis of Poplar SQUAMOSA-Promoter-Binding Protein (SBP) Family under Salt Stress

Forests ◽  
2021 ◽  
Vol 12 (4) ◽  
pp. 413
Author(s):  
Qing Guo ◽  
Li Li ◽  
Kai Zhao ◽  
Wenjing Yao ◽  
Zihan Cheng ◽  
...  
Keyword(s):  
Salt Stress ◽  
Abiotic Stress ◽  
Stress Responses ◽  
Growth And Development ◽  
Binding Protein ◽  
Gene Segment ◽  
Gene Expression Pattern ◽  
Genome Wide Analysis ◽  
Genome Wide ◽  
Squamosa Promoter Binding Protein

SQUAMOSA promoter binding protein (SBP) is a kind of plant-specific transcription factor, which plays a crucial role in stress responses and plant growth and development by activating and inhibiting the transcription of multiple target genes. In this study, a total of 30 SBP genes were identified from Populus trichocarpa genome and randomly distributed on 16 chromosomes in poplar. According to phylogenetic analysis, the PtSBPs can be divided into six categories, and 14 out of the genes belong to VI. Furthermore, the SBP genes in VI were proved to have a targeting relationship with miR156. The homeopathic element analysis showed that the promoters of poplar SBP genes mainly contain the elements involved in growth and development, abiotic stress and hormone response. In addition, there existed 10 gene segment duplication events in the SBP gene duplication analysis. Furthermore, there were four poplar and Arabidopsis orthologous gene pairs among the poplar SBP members. What is more, poplar SBP gene family has diverse gene expression pattern under salt stress. As many as nine SBP members were responding to high salt stress and six members possibly participated in growth development and abiotic stress. Yeast two-hybrid experiments indicated that PtSBPs can form heterodimers to interact in the transcriptional regulatory networks. The genome-wide analysis of poplar SBP family will contribute to function characterization of SBP genes in woody plants.

scholarly journals A Distal Region Involving Hepatocyte Nuclear Factor 4α and CAAT/Enhancer Binding Protein Markedly Potentiates the Protein Kinase A Stimulation of the Glucose-6-Phosphatase Promoter

2005 ◽  
Vol 19 (1) ◽  
pp. 163-174 ◽  
Author(s):  
Amandine Gautier-Stein ◽  
Gilles Mithieux ◽  
Fabienne Rajas
Keyword(s):  
Protein Kinase ◽  
Protein Kinase A ◽  
Binding Sites ◽  
Binding Protein ◽  
Distal Region ◽  
Proximal Region ◽  
Nuclear Factor ◽  
Hepatocyte Nuclear Factor ◽  
Enhancer Binding Protein ◽  
Kinase A

Abstract Glucose-6-phosphatase (Glc6Pase) is the last enzyme of gluconeogenesis and is only expressed in the liver, kidney, and small intestine. In these tissues, the mRNA and its activity are increased when cAMP levels increased (e.g. in fasting or diabetes). We first report that a proximal region (within −200 bp relative to the transcription start site) and a distal region (−694/−500 bp) are both required for a potent cAMP and a protein kinase A (PKA) responsiveness of the Glc6Pase promoter. Using different molecular approaches, we demonstrate that hepatocyte nuclear factor (HNF4α), CAAT/ enhancer-binding protein-α (C/EBPα), C/EBPβ, and cAMP response element-binding protein (CREB) are involved in the potentiated PKA responsiveness: in the distal region, via one HNF4α- and one C/EBP-binding sites, and in the proximal region, via two HNF4α and two CREB-binding sites. We also show that HNF4α, C/EBPα, and C/EBPβ are constitutively bound to the endogenous Glc6Pase gene, whereas CREB and CREB-binding protein (CBP) will be bound to the gene upon stimulation by cAMP. These data strongly suggest that the cAMP responsiveness of the Glc6Pase promoter requires a tight cooperation between a proximal and a distal region, which depends on the presence of several HNF4α-, C/EBP-, and CREB-binding sites, therefore involving an intricate association of hepatic and ubiquitous transcription factors.

Vitamin D-binding protein: multifunctional component of blood serum

2021 ◽  
Vol 76 (1) ◽  
pp. 103-110
Author(s):  
Alexandra A. Povaliaeva ◽  
Ekaterina A. Pigarova ◽  
Anastasia A. Romanova ◽  
Larisa K. Dzeranova ◽  
Artem Y. Zhukov ◽  
...  
Keyword(s):  
Vitamin D ◽  
Binding Sites ◽  
Binding Protein ◽  
Vitamin D Metabolites ◽  
Biological Functions ◽  
Vitamin D Binding Protein ◽  
Fatty Acid Binding ◽  
Physiological Properties ◽  
Steroid Binding ◽  
Tumor Pathogenesis

Vitamin D-binding protein (DBP) was discovered more than half a century ago as a polymorphic serum protein and is currently characterized by a variety of physiological properties. First of all, DBP carries the bulk of vitamin D metabolites circulating in the bloodstream, while albumin is the second most important transport protein, especially in patients with a low concentration of DBP in serum. Since it was discovered that only 12% of the total circulating DBP have occupied steroid binding sites, a vigorous study of other potential biological roles of DBP was initiated: actin utilization, regulation of inflammation and innate immunity mechanisms, fatty acid binding, effects on bone metabolism and participation in the tumor pathogenesis. This review focuses on the main known biological functions of DBP.

Intact Ca(2+)-binding sites are required for targeting of annexin 1 to endosomal membranes in living HeLa cells

2000 ◽  
Vol 113 (22) ◽  
pp. 3931-3938 ◽  
Author(s):  
U. Rescher ◽  
N. Zobiack ◽  
V. Gerke
Keyword(s):  
Hela Cells ◽  
Binding Sites ◽  
Fluorescent Protein ◽  
Binding Protein ◽  
Membrane Binding ◽  
Growth Factor Receptor ◽  
Intracellular Distribution ◽  
Live Cells ◽  
Membrane Structures ◽  
Annexin 1

Annexin 1 is a Ca(2+)-regulated membrane binding protein and a major substrate of the epidermal growth factor receptor kinase. Because of its properties and intracellular distribution, the protein has been implicated in endocytic trafficking of the receptor, in particular in receptor sorting occurring in multivesicular endosomes. Up to now, however, the localization of annexin 1 to cellular membranes has been limited to subcellular fractionation and immunocytochemical analyses of fixed cells. To establish its localization in live cells, we followed the intracellular fate of annexin 1 molecules fused to the Green Fluorescent Protein (GFP). We show that annexin 1-GFP associates with distinct, transferrin receptor-positive membrane structures in living HeLa cells. A GFP chimera containing the Ca(2+)/phospholipid-binding protein core of annexin 1 also shows a punctate intracellular distribution, although the structures labeled here do not resemble early but, at least in part, late endosomes. In contrast, the cores of annexins 2 and 4 fused to GFP exhibit a cytoplasmic or a different punctate distribution, respectively, indicating that the highly homologous annexin core domains carry distinct membrane specificities within live cells. By inactivating the three high-affinity Ca(2+) binding sites in annexin 1 we also show that endosomal membrane binding of the protein in live HeLa cells depends on the integrity of these Ca(2+) binding sites. More detailed analysis identifies a single Ca(2+) site in the second annexin repeat that is crucially involved in establishing the membrane association. These results reveal for the first time that intracellular membrane binding of an annexin in living cells requires Ca(2+) and is mediated in part through an annexin core domain that is capable of establishing specific interactions.

Sign in / Sign up

Export Citation Format

Share Document