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1.
Sci Rep ; 9(1): 9601, 2019 07 03.
Article in English | MEDLINE | ID: mdl-31270425

ABSTRACT

Gibberellins (GA) are key positive regulators of seed germination. Although the GA effects on seed germination have been studied in a number of species, little is known about the transcriptional reprogramming modulated by GA during this phase in species other than Arabidopsis thaliana. Here we report the transcriptome analysis of soybean embryonic axes during germination in the presence of paclobutrazol (PBZ), a GA biosynthesis inhibitor. We found a number of differentially expressed cell wall metabolism genes, supporting their roles in cell expansion during germination. Several genes involved in the biosynthesis and signaling of other phytohormones were also modulated, indicating an intensive hormonal crosstalk at the embryonic axis. We have also found 26 photosynthesis genes that are up-regulated by PBZ at 24 hours after imbibition (HAI) and down-regulated at 36 HAI, which led us to suggest that this is part of a strategy to implement an autotrophic growth program in the absence of GA-driven mobilization of reserves. Finally, 30 transcription factors (mostly from the MYB, bHLH, and bZIP families) were down-regulated by PBZ and are likely downstream GA targets that will drive transcriptional changes during germination.


Subject(s)
Gene Expression Regulation, Plant/drug effects , Germination/drug effects , Gibberellins/antagonists & inhibitors , Glycine max/genetics , Triazoles/pharmacology , Arabidopsis/genetics , Arabidopsis/metabolism , Arabidopsis Proteins/genetics , Arabidopsis Proteins/metabolism , Gibberellins/metabolism , Photosynthesis/drug effects , Plant Growth Regulators/antagonists & inhibitors , Plant Growth Regulators/metabolism , Plant Proteins/genetics , Plant Proteins/metabolism , Seeds/genetics , Seeds/growth & development , Seeds/metabolism , Glycine max/growth & development , Glycine max/metabolism , Transcription Factors/genetics , Transcription Factors/metabolism
2.
PLoS One ; 11(4): e0153528, 2016.
Article in English | MEDLINE | ID: mdl-27064899

ABSTRACT

Somatic embryogenesis has been shown to be an efficient tool for studying processes based on cell growth and development. The fine regulation of the cell cycle is essential for proper embryo formation during the process of somatic embryogenesis. The aims of the present work were to identify and perform a structural and functional characterization of Mps1 and to analyze the effects of the inhibition of this protein on cellular growth and pro-embryogenic mass (PEM) morphology in embryogenic cultures of A. angustifolia. A single-copy Mps1 gene named AaMps1 was retrieved from the A. angustifolia transcriptome database, and through a mass spectrometry approach, AaMps1 was identified and quantified in embryogenic cultures. The Mps1 inhibitor SP600125 (10 µM) inhibited cellular growth and changed PEMs, and these effects were accompanied by a reduction in AaMps1 protein levels in embryogenic cultures. Our work has identified the Mps1 protein in a gymnosperm species for the first time, and we have shown that inhibiting Mps1 affects cellular growth and PEM differentiation during A. angustifolia somatic embryogenesis. These data will be useful for better understanding cell cycle control during somatic embryogenesis in plants.


Subject(s)
Cell Proliferation , Plant Proteins/antagonists & inhibitors , Plant Somatic Embryogenesis Techniques , Tracheophyta/embryology , Tracheophyta/metabolism , Cell Culture Techniques , Plant Proteins/genetics , Plant Proteins/metabolism , Tracheophyta/chemistry , Transcriptome
3.
J Agric Food Chem ; 64(18): 3514-22, 2016 May 11.
Article in English | MEDLINE | ID: mdl-27078512

ABSTRACT

The seed coat is an external tissue that participates in defense against insects. In some nonhost seeds, including Albizia lebbeck, the insect Callosobruchus maculatus dies during seed coat penetration. We investigated the toxicity of A. lebbeck seed coat proteins to C. maculatus. A chitin-binding protein fraction was isolated from seed coat, and mass spectrometry showed similarity to a C1 cysteine protease. By ELM program an N-glycosylation interaction motif was identified in this protein, and by molecular docking the potential to interact with N-acetylglucosamine (NAG) was shown. The chitin-binding protein fraction was toxic to C. maculatus and was present in larval midgut and feces but not able to hydrolyze larval gut proteins. It did not interfere, though, with the intestinal cell permeability. These results indicate that the toxicity mechanism of this seed coat fraction may be related to its binding to chitin, present in the larvae gut, disturbing nutrient absorption.


Subject(s)
Albizzia/chemistry , Chitin/metabolism , Insect Proteins/metabolism , Plant Proteins/metabolism , Weevils/drug effects , Albizzia/metabolism , Albizzia/parasitology , Animals , Larva/drug effects , Larva/metabolism , Plant Proteins/toxicity , Protein Binding , Seeds/chemistry , Seeds/metabolism , Seeds/parasitology , Weevils/metabolism
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