PEP444c encoded within MIR444c gene regulates microRNA444c accumulation in barley
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ABSTRACT:
PROVIDER: PRJNA955714 | ENA |
REPOSITORIES: ENA
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Project description:Mutations in the PEP444c coding region have an impact on the accumulation of corresponding microRNA. The level of microRNA444c is decreased in roots of pep444c-332.10 mutant plants compared to WT plants, whereas the level of microRNA444c in shoots was unchanged. Results indicate a significant effect of PEP444c on the accumulation of microRNA444c in roots.
2025-02-24 | GSE229727 | GEO
Project description:The temporal pattern of accumulation of hordein storage proteins in developing barley grains was studied by enzyme-linked immunosorbent assay (ELISA), western blot and liquid chromatography tandem mass spectrometry (LC-MS/MS). Hordein accumulation was compared to the pattern seen for two abundant control proteins, serpin Z4 (an early accumulator) and lipid transferase protein (LTP1, a late accumulator). Hordeins were detected from six days post-anthesis (DPA) and peaked at 30 DPA. Changes in fresh weight indicate that desiccation begins at 20 DPA and by 37 DPA fresh weight had decreased by 35%. ELISA analysis of hordein content, expressed on a protein basis, increased to a maximum at 30 DPA followed by a 17% decrease by 37 DPA. The accumulation of 39 tryptic and 29 chymotryptic hordein peptides representing all classes of hordein was studied by LC-MS/MS. Most peptides increased to a maximum at 30 DPA, and either remained at the maximum or did not decrease significantly. Only five tryptic peptides, members of the related B1- and γ1-hordeins decreased significantly by 21-51% at 37 DPA. Thus, the concentration of some specific peptides wasere reduced while remaining members of the same family were not affected. The N-terminal signal region was removed by proteolysis during co-translation. , evidenced by a notable absence of the predicted peptides despite near complete protein sequence coverage. In addition to a suite of previously characterised hordeins, two novel barley B-hordein isoforms and two avenin-like proteins (ALPs), mapping to wheat low molecular weight glutenins (LMW-GS-like B-hordeins), and two avenin-like proteins (ALPs) sharing homology with wheat ALPs, were identified. These identified isoforms have not previously been mapped in the barley genome. Cereal storage proteins provide significant nutritional content for human consumption and seed germination. In barley, the bulk of the storage proteins are due tocomprise the hordein family and the final hordein concentration affects the quality of baked and brewed products. Hordeins are members of the gluten protein family and consumption can trigger health conditions such as coeliac disease, non-coeliac gluten sensitivity, and gluten allergy. It is therefore important to study the accumulation of these proteinshordeins as this knowledge may assist plant breeding for improved health outcomes (by minimizing triggering of detrimental immune responses), nutrition and food reduced coeliac reactivity.processing properties.
2019-04-18 | PXD013331 | Pride
Project description:Effect of high grain protein locus on barley grain protein accumulation. Gene expression levels were analysed in Karl, a low grain protein variety with its near-isogenic line 10_11(has high grain protein locus, chromosome 6)using Barley1 22k affymetrix chip. ****[PLEXdb(http://www.plexdb.org) has submitted this series at GEO on behalf of the original contributor, Aravind Jukanti. The equivalent experiment is BB53 at PLEXdb.]
2011-11-22 | GSE33413 | GEO
Project description:LINC00266-1-encoded peptide regulates mRNA splicing
| PRJNA527803 | ENA
Project description:LOC90024-encoded small protein SRSP regulates mRNA splicing
| PRJNA579559 | ENA
Project description:Comparison of mRNA accumulation in segregating doubled haploid barley lines ****[PLEXdb(http://www.plexdb.org) has submitted this series at GEO on behalf of the original contributor, . The equivalent experiment is BB21 at PLEXdb.]
2011-11-22 | GSE33394 | GEO
Project description:Chlorophyll production involves the synthesis of photoreactive intermediates that are toxic when in excess due to the production of reactive oxygen species (ROS). A novel activation tagged barley mutant is described that results from antisense suppression of a uroporphyrinogen III synthase (Uros) gene, the product of which catalyses the sixth step in the synthesis of chlorophyll and heme. In homozygous mutant plants uroporphyrin(ogen) I accumulates by spontaneous cyclization of hydroxyl methylbilane, the substrate of Uros. Accumulation of this tetrapyrrole intermediate results in photosensitive cell death due to the production of reactive oxygen species. The efficiency of Uros gene suppression is developmentally regulated, being most effective in mature seedling leaves compared with newly emergent leaves. A comparison of RNA from mutant and wild type seedlings grown under 30% and 3% light, shows reduced transcript accumulation of a number of nuclear-encoded photosynthesis genes occurs in the mutant even under 3% light conditions. This is consistent with a retrograde plastid-nuclear signalling mechanism arising from Uros gene suppression. No evidence for a direct signalling role by uroporphyrin I was observed suggesting that nuclear gene transcriptional suppression was mediated by ROS accumulation. Two replicates samples were used for barley mutant 70a3 grown under 3% and 2 replicate sample of the mutant grown under 30% light, barley cv Golden Promise was used as the control.
2009-04-23 | E-GEOD-11776 | biostudies-arrayexpress
Project description:Comparison of mRNA accumulation in the seedling leaves of 8 unstressed barley cultivars ****[PLEXdb(http://www.plexdb.org) has submitted this series at GEO on behalf of the original contributor, . The equivalent experiment is BB20 at PLEXdb.]
2011-11-22 | GSE33393 | GEO
Project description:Mitochondria are known to be functional organelles, but their role as a signaling unit is increasingly being appreciated. The recent identification of a short open reading frame (sORF) in the mitochondrial DNA (mtDNA) that encodes a signaling peptide, humanin, suggests the possible existence of additional sORFs in the mtDNA that yield bioactive peptides. Here we report the identification of a sORF within the mitochondrial 12S rRNA encoding a 16-amino-acid peptide named MOTS-c (mitochondrial open-reading-frame of the twelve S rRNA -c) that regulates insulin sensitivity and metabolic homeostasis. MOTS-c is detected in various tissues and in circulation in an age-dependent manner. Its primary target organ appears to be the skeletal muscle and its cellular actions inhibit the folate cycle and its tethered de novo purine biosynthesis, causing a significant accumulation of AICAR levels concomitantly with AMPK activation. MOTS-c treatment in mice prevented age-dependent and high-fat diet-induced insulin resistance, as well as diet-induced obesity. These results suggest that mitochondria may be more actively engaged in regulating metabolic homeostasis than previously recognized, through the production of peptides encoded within its genome that act at the cellular and organismal level. Human embryonic kidney cells (HEK293 cell line) were cultured in 10-cm dishes in 7 mL of phenol-free DMEM supplemented with 10% FBS and incubated with water (controls) or the 16-amino-acid peptide mitochondrial open-reading-frame of the twelve S rRNA-c (MOTS-c, 10 uM) for 4 or 72 hours prior to RNA extraction.
2015-03-07 | E-GEOD-65068 | biostudies-arrayexpress
Project description:Caryopses of barley (Hordeum vulgare), like all other cereal seeds, are complex sink organs optimized for storage starch accumulation and embryo development. Their development from early stages after pollination to late stages of seed ripening has been studied in great detail. However, information on the caryopses’ diurnal adaptation to changes in light, temperature and alterations in phloem-supplied carbon and nitrogen remained unknown. In this study, we applied the 22K Barley1 GeneChip microarray to investigate diurnal gene regulation events of barley caryopses at 11 to 12 days post anthesis.
2010-03-25 | GSE20034 | GEO