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ADHERENT1 IS A 3-KETOACYL CoA SYNTHASE REQUIRED FOR MAIZE CUTICLE DEVELOPMENT AND ORGAN SEPARATION

ABSTRACT: ADHERENT1 IS A 3-KETOACYL CoA SYNTHASE REQUIRED FOR MAIZE CUTICLE DEVELOPMENT AND ORGAN SEPARATION

PROVIDER: PRJNA598606 | ENA |

REPOSITORIES: ENA

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ADHERENT1 IS A 3-KETOACYL CoA SYNTHASE REQUIRED FOR MAIZE CUTICLE DEVELOPMENT AND ORGAN SEPARATION

Project description:DAP-seq was used to generate genome-wide DNA:TF interaction maps for ZmMYB94/FDL1

2020-06-01 | GSE142847 | GEO

THE FUSED LEAVES1-ADHERENT1 REGULATORY MODULE IS REQUIRED FOR MAIZE CUTICLE DEVELOPMENT AND ORGAN SEPARATION

Project description:THE FUSED LEAVES1-ADHERENT1 REGULATORY MODULE IS REQUIRED FOR MAIZE CUTICLE DEVELOPMENT AND ORGAN SEPARATION

| PRJNA629302 | ENA

The FUSED LEAVES1-ADHERENT1 regulatory module is required for maize cuticle development and organ separation.

Project description:All aerial epidermal cells in land plants are covered by the cuticle, an extracellular hydrophobic layer that provides protection against abiotic and biotic stresses and prevents organ fusion during development. Genetic and morphological analysis of the classic maize adherent1 (ad1) mutant was combined with genome-wide binding analysis of the maize MYB transcription factor FUSED LEAVES1 (FDL1), coupled with transcriptional profiling of fdl1 mutants. We show that AD1 encodes an epidermally-expressed 3-KETOACYL-CoA SYNTHASE (KCS) belonging to a functionally uncharacterized clade of KCS enzymes involved in cuticular wax biosynthesis. Wax analysis in ad1 mutants indicates that AD1 functions in the formation of very-long-chain wax components. We demonstrate that FDL1 directly binds to CCAACC core motifs present in AD1 regulatory regions to activate its expression. Over 2000 additional target genes of FDL1, including many involved in cuticle formation, drought response and cell wall organization, were also identified. Our results identify a regulatory module of cuticle biosynthesis in maize that is conserved across monocots and eudicots, and highlight previously undescribed factors in lipid metabolism, transport and signaling that coordinate organ development and cuticle formation.

| S-EPMC7754373 | biostudies-literature

THE FUSED LEAVES1-ADHERENT1 REGULATORY MODULE IS REQUIRED FOR MAIZE CUTICLE DEVELOPMENT AND ORGAN SEPARATION

Project description:RNA-seq was performed on 3-4mm WT and fdl1 mutant maize coleoptile tips

2020-08-06 | GSE149577 | GEO

SWATH-MS analysis of transgenic tobacco overexpressing 3-hydroxy-3-methylglutaryl-CoA synthase

Project description:3-Hydroxy-3-methylglutaryl-CoA synthase (HMGS) is the second enzyme in the mevalonate pathway. While the recombinant Brassica juncea HMGS1 (BjHMGS1) mutant S359A displayed 10-fold higher enzyme activity than wild-type (wt) BjHMGS1, transgenic tobacco overexpressing S359A (OE-S359A) exhibited greater sterol content, growth rate and seed yield than OE-wtBjHMGS1. To explore the mechanism of HMGS and its mutant (S359A) in promotion of plant growth, SWATH-MS quantitative proteomics analysis was performed.

2021-01-04 | PXD006869 | Pride

SWATH-MS analysis of 3-hydroxy-3-methylglutaryl-CoA synthase specific inhibitor (F-244)-treated Arabidopsis

Project description:3-Hydroxy-3-methylglutaryl-CoA synthase (HMGS) is the second enzyme in the mevalonate pathway. F-244 is the specific inhibitor of HMGS. F-244 treatment caused reduced primary root growth. SWATH-MS quantitative proteomics analysis was carried out to identify differential expressed proteins in F-244-treated primary roots.

2019-10-01 | PXD009776 | Pride

The Daphnia cuticle proteome - whole cuticle samples

Project description:The cuticles of arthropods, including aquatic crustaceans like Daphnia, provide an interface between the organism and its environment. Thus, the cuticle’s structure influences how the organism responds to and interacts with its surroundings. Here, we used label-free quantification proteomics to provide a proteome of the molted cuticle of Daphnia magna, which has long been a prominent subject of studies on ecology, evolution, and developmental biology, anddetected 278 high confidence proteins. Using protein sequence domain and functional enrichment analyses, we identified chitin-binding structural proteins and chitin modifying enzymes as most abundant protein groups in the cuticle proteome.Structural cuticular protein families showed a similar distribution to those found in other arthropods and indicated proteins responsible for the soft and flexible structure of the Daphnia cuticle . Finally, cuticle protein genes were clustered as tandem gene arrays in the Daphnia genome, indicating their importance for adaptation to environmental change. The cuticle proteome presented here will be a valuable resource to the Daphnia research community, informing investigations on diverse topics such as the genetic basis of interactions with predators and parasites.

2024-09-02 | PXD040228 | Pride

The Daphnia cuticle proteome - partial cuticle samples

2024-09-02 | PXD040304 | Pride

Protein Acetylation data for Lin et al, "CoA Synthase Regulates Mitotic Fidelity via CBP-Mediated Acetylation", Nat. Commun. 2018

Project description:Protein acetylation was analyzed in A549 cell line upon siRNA silencing of COASY protein. Supplementary Discovery Data for "CoA Synthase Regulates Mitotic Fidelity via CBP-Mediated Acetylation", Lin et al, Nature Communications 2018.

2018-01-15 | MSV000081937 | MassIVE

Functional cooperation of glycine synthase-reductase pathway with Wood-Ljungdahl pathway for autotrophic growth of Clostridium drakei

Project description:The Wood-Ljungdahl pathway in acetogens converts C1 compounds, such as CO2 and CO, into acetyl-CoA. Similarly, the glycine synthase pathway assimilates C1 compounds into glycine. Partial glycine synthase genes are widely conserved in the Wood-Ljungdahl pathway gene cluster but functional relationship between the pathways in autotrophic condition remains unknown. To comprehend, we assembled Clostridium drakei genome (5.7-Mbp) with intact glycine synthase pathway and constructed a genome-scale metabolic model, iSL836, predicting increased metabolic flux rates of the Wood-Ljungdahl pathway and the glycine synthase-reductase associated reactions under autotrophic conditions. Along with the observation of significant transcriptional activation of genes in the pathways, surprisingly, 13C-labeling experiments and enzyme activity assays confirmed the strain synthesizes glycine and converts into acetyl-phosphate. This study suggests the Wood-Ljungdahl and the glycine synthase-reductase pathways convert CO2 into acetyl-CoA and acetyl-phosphate, respectively. In our knowledge, this is the first report on co-utilization of the pathways under autotrophic growth in acetogen.

2019-08-01 | GSE118519 | GEO

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