Expression data from rice 10DAF developing seeds from wildtype and strains with high lysine levels
Ontology highlight
ABSTRACT:
ORGANISM(S): Oryza sativa
PROVIDER: GSE109486 | GEO | 2018/01/24
REPOSITORIES: GEO
Similar Datasets
Project description:Developing Evans seeds at 25, 30, 40, 45 and 50 days after flowering (DAF) were harvested and analyzed to gain insights as to the biochemical program that determines soybean seed development. We used microarrays to detail the global programme of gene expression underlying seed development and identified distinct classes of genes with changed expression during this process.
2014-09-11 | GSE61350 | GEO
Project description:Developing Evans seeds at 25, 30, 40, 45 and 50 days after flowering (DAF) were harvested and analyzed to gain insights as to the biochemical program that determines soybean seed development. We used microarrays to detail the global programme of gene expression underlying seed development and identified distinct classes of genes with changed expression during this process. Sampled developing Evans seeds at 25, 30, 40, 45 and 50 days after flowering (5 time points), with two replicates each.
2014-09-11 | E-GEOD-61350 | biostudies-arrayexpress
Project description:Expression data from rice 10DAF developing seeds from wildtype and strains with high lysine levels
| PRJNA431199 | ENA
Project description:Lysine succinylation has been recognized as a post-translational modification (PTM) in recent years. It is plausible that succinylation may have a vaster functional impact than acetylation due to bulkier structural changes and greater charge differences on the modified lysine residue. Currently, however, the quantity of identified succinylated proteins and their corresponding functions in cereal plants remain largely unknown. In this study, 854 lysine succinylation sites on 347 proteins have been identified by a thorough investigation in developing rice seeds. Six motifs were revealed as preferred amino-acid sequence arrangements for succinylation sites, and a noteworthy motif preference was discovered in proteins associated with different biological processes, molecular functions, pathways, and domains. Remarkably, heavy succinylation was detected on major seed storage proteins, in conjunction with key enzymes involved in central carbon metabolism and starch biosynthetic pathways for rice seed development. Conserved succinylated proteins were identified amongst varying organisms. Rice proteins with co-modifications of succinylation, acetylation, malonylation, crotonylation, and 2-hydroxyisobutyrylation were identified through a comprehensive comparison analysis. A striking number of highly conserved succinyl-proteins and multi-modified proteins were shown to be involved in vital metabolic events. Our study delivers a platform for expansive investigation of molecular networks administrating cereal seed development via PTMs.
2019-09-09 | PXD013664 | Pride
Project description:Lysine 2-hydroxyisobutyrylation is a recently identified protein post-translational modification that is known to affect the association between histone and DNA. However, non-histone protein lysine 2-hydroxyisobutyrylation remains largely unexplored. Utilizing antibody-based affinity enrichment and nano-HPLC/MS/MS analyses of 2-hydroxyisobutyrylation peptides, we efficaciously identified 9,916 2-hydroxyisobutyryl lysine sites on 2,512 proteins in developing rice seeds, representing the first lysine 2-hydroxyisobutyrylome dataset in plants. Functional annotation analyses indicated that a wide variety of vital biological processes were preferably targeted by lysine 2-hydroxyisobutyrylation, including glycolysis/gluconeogenesis, TCA cycle, starch biosynthesis, lipid metabolism, protein biosynthesis and processing. Our finding showed that 2-hydroxyisobutyrylated histone sites were conserved across plants, human, and mouse. A number of 2-hydroxyisobutyryl sites were shared with other lysine acylations in both histone and non-histone proteins. Comprehensive analysis of the lysine 2-hydroxyisobutyrylation sites illustrated that the modification sites were highly sequence specific with distinct motifs, and they had less surface accessibility than other lysine residues in the protein. Overall, our study provides the first systematic analysis of lysine 2-hydroxyisobutyrylation proteome in plants, and it serves as an important resource for future investigations of the regulatory mechanisms and functions of lysine 2-hydroxyisobutyrylation.
| S-EPMC5727541 | biostudies-literature
Project description:Lysine succinylation has been recognized as a post-translational modification (PTM) in recent years. It is plausible that succinylation may have a vaster functional impact than acetylation because of bulkier structural changes and more significant charge differences on the modified lysine residue. Currently, however, the quantity and identity of succinylated proteins and their corresponding functions in cereal plants remain largely unknown. In this study, we estimated the native succinylation occupancy on lysine was between 2% to 10% in developing rice seeds. Eight hundred fifty-four lysine succinylation sites on 347 proteins have been identified by a thorough investigation in developing rice seeds. Six motifs were revealed as preferred amino acid sequence arrangements for succinylation sites, and a noteworthy motif preference was identified in proteins associated with different biological processes, molecular functions, pathways, and domains. Remarkably, heavy succinylation was detected on major seed storage proteins, in conjunction with critical enzymes involved in central carbon metabolism and starch biosynthetic pathways for rice seed development. Meanwhile, our results showed that the modification pattern of in vitro nonenzymatically succinylated proteins was different from those of the proteins isolated from cells in Western blots, suggesting that succinylation is not generated via nonenzymatic reaction in the cells, at least not completely. Using the acylation data obtained from the same rice tissue, we mapped many sites harboring lysine succinylation, acetylation, malonylation, crotonylation, and 2-hydroxisobutyrylation in rice seed proteins. A striking number of proteins with multiple modifications were shown to be involved in critical metabolic events. Given that these modification moieties are intermediate products of multiple cellular metabolic pathways, these targeted lysine residues may mediate the crosstalk between different metabolic pathways via modifications by different moieties. Our study exhibits a platform for extensive investigation of molecular networks administrating cereal seed development and metabolism via PTMs.
| S-EPMC6885699 | biostudies-literature
Project description:Carbon (C) and nitrogen (N) contents of grain-filling stage are keys item that determined the growth of rice, and also the quality of seed. Therefore, to elucidating the mechanism of C/N signaling in a seed is an important problem for crops whose seed is used as food like rice. The DNA microarray analysis with the rice seed which was performed the additional fertilizer at the time of heading, in order to clarify how C/N signal change of the rhizosphere in seed production stage affects a seed component on a gene expression level.
2014-08-04 | GSE49818 | GEO
Project description:Seed development, which depends on mother plant genetic background and environmental conditions, is a major component determining seed composition. Seed quality is a main agricultural concern, impacting both food and non-food applications, while also playing a central role in biodiversity conservation and environment protection. Climate change, characterized, among other stresses, by the emergence of extremely high temperatures, constitute a critical global threat to agriculture. Specialized metabolites (SMs) play crucial roles in the interactions of plants and seeds with their environments. Several SMs are known to be protective compounds involved in seed stress responses, thus impacting directly or indirectly their quality. In this study, we performed untargeted metabolomic (LC-MS/MS) and transcriptomic (RNA-Seq) analyses of Arabidopsis thaliana seeds harvested at six developmental stages (Globular, Transition, Torpedo, Bent cotyledon, Mature green and Dry seed), and developed under control and warm temperature conditions. Those data provide an original and valuable resource for future studies on the role of SMs and genes involved in seed warm thermic stress responses and for the study of their regulation and functions during seed development.
| MSV000095846 | MassIVE
Project description:Arabidopsis seeds expressing the castor fatty acid hydroxylase accumulate hydroxylated fatty acids up to 17% of total fatty acids in seed triacylglycerols, however total seed oil is also reduced up to 50%. Investigations into the cause of the reduced oil phenotype through in vivo [14C]acteate and [3H]2O metabolic labeling of developing seeds surprisingly revealed that the rate of de novo fatty acid synthesis within the transgenic seeds was approximately half that of control seeds. Addition of castor phospholipid:diacylglycerol acyltransferase (PDAT) increased hydroxylated fatty acid content of the seed oil, increased the rate of fatty acid synthesis, and mostly restored seed oil levels. RNAseq analysis indicated no changes in expression of fatty acid synthesis genes in hydroxylase-expressing plants.
2014-01-10 | GSE53952 | GEO
Project description:Transcriptomic analysis of maintenance of dormancy induced by seed development temperature We used Affymetrix GeneChip Wheat Genome Array to detail transcriptional programs underlying maintenance of dormancy induced by seed development tempearture in imbibing seeds of wheat
2021-06-30 | GSE153527 | GEO