Floral nectar metagenome
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA351801 | ENA |
REPOSITORIES: ENA
Similar Datasets
Project description:Floral nectar is a rich secretion produced by nectaries offered as an attractive reward to pollinators. Floral nectaries secrete an aqueous solution largely composed of sugars and amino acids as well as an array of proteins called nectarins. These provide one of the main mechanisms of floral defense in Nicotiana nectar. Due to its composition, floral nectar provides an ideal source of nutrients for specialized microorganisms that can change the nectar composition. Understanding of floral defenses and the role of nectar proteins is essential to predict the impacts in microbial growth, nectar composition, and relationships between plants and pollinators. In order to deepen knowledge about Nicotiana spp. nectar proteins, we used LC-MS/MS-based comparative proteomic analysis to identify 22 proteins from Petunia hybrida, 35 proteins from Datura stramonium, and 144 proteins from 23 different species of Nicotiana. GO enrichment analysis and secretory signal peptide prediction demonstrated that defense/stress was the largest group of proteins in nectars with differential abundance and distribution throughout genus Nicotiana. The Nicotiana spp. proteome consisted of 105 exclusive proteins such as lipid transfer proteins (LTPs), Nectar Redox Cycle proteins, proteases inhibitors (PI), and PR-proteins. Analysis by taxonomic sections demonstrated that LTPs were the most abundant group of proteins in the nectar of Undulatae and Noctiflora sections while nectarins were more abundant proteins in Rusticae, Suaveolens, Polydicliae, and Alata sections. Peroxidases (Pox) and chitinases (Chit) were exclusive to P. hybrida nectar, while D. stramonium proteome had only seven unique proteins. Significant differences were identified between the proteome of taxonomic sections providing relevant insights into the group of proteins related to defense/stress associated with Nectar Redox Cycle, antimicrobial proteins and signaling pathways. The activity of floral nectar proteins is suggested impact the microbial growth. The knowledge about these proteomes provides significant insights into the diversity of proteins secreted in the nectars and the array of mechanisms used by Nicotiana spp. in its floral defense.
2020-01-08 | PXD014760 | Pride
Project description:Nectar from Nicotiana plants targeted loci
| PRJNA301508 | ENA
Project description:Many angiosperms can secret at least two types of sugar-rich liquids, floral nectar (FN) and extrafloral nectar (EFN), by which plants can make use of the animal partner’s mobility for pollen transportation and attract predatory animals for indirect defense. Both FN and EFN contain considerable amount of proteins which play important roles in nectar biosynthesis process and protection. Hemerocallis citrina (HC) can secrete both FN and EFN on flower during the same developmental stage. Our objective was to compare the HC FN and EFN proteome to understand the difference between their biosynthesis and ecological function. FN was collected from adult HC flowers and concentrated by ultrafiltering. EFN was collected from young HC flower buds and concentrated by ultrafiltering. Proteins were digested with trypsin then analyzed by LC-MS/MS. HSPs are the main protein identified in HC FN but their function in floral nectar is still largely unknown. PR proteins are the main protein identified in HC EFN with antimicrobial activity. Our data provide a good characterization of a monocot nectar proteome. These data, may be useful in understanding the generation process and ecological function of floral and extrafloral nectar.
2023-03-11 | PXD025892 | Pride
Project description:Priority effects persists across floral generations in nectar microbial metacommunities
| PRJDB4972 | ENA
Project description:Label-free quantitative proteome analysis of extrafloral (EFN) and floral nectar (FN) from castor (Ricinus communis) plants.
2018-10-19 | PXD009104 | Pride
Project description:Floral nectar proteins (nectarins) are mainly enzymes and play important roles in inhibiting microbial growth in nectar and tailoring nectar chemistry before or after secretory. Nectar proteomes are usually small, but only very few plant species have had their nectar proteomes thoroughly investigated. Nectarins from Nicotiana tabacum (NT) were separated using two-dimensional gel electrophoresis, and then analyzed using mass spectrometry. Glycoproteins were isolated from raw NT nectar, separated by SDS-PAGE, and identified by mass spectrometry. All eight identified nectarins and four invertase genes’ expression were analysed by qPCR. Sugars composition, total sugar concentration, protein content, polyphenol content and hydrogen peroxide content were compared at different time intervals in extracted nectar and nectar in situ after secretion. Totally, eight nectarins were detected in NT nectar in which only two are glycoproteins, beta-xylosidase and a protein with unknown function. All of the eight nectarin genes expression was not nectary-specific and not synchronous along with the nectary development. After secretion, NT nectar in flower tube changed from sucrose–rich to hexose-rich type even though no free invertase or its activity was detected in NT nectar. No sugar composition changes observed in extracted nectar after incubating at 30 ℃ up to 48 hours in plastic tubes. Our results indicate that nectar post-secretory changes could be a complex process and tissue closely contact with nectar might function in it.
2019-08-20 | PXD011658 | Pride
Project description:Nectaries are the glands responsible for nectar secretion. To understand the genetic programming underlying nectar production, floral nectaries of six Nicotiana species at four different time points (floral stage 6,9, and 12, a post-secretory stage) in biological triplicate were collected, with RNA being isolated and subjected to Illumina RNA-seq analysis.
2018-04-12 | GSE112526 | GEO
Project description:Floral nectar plays important roles in the interaction between animal-pollinated plants and pollinators. Growing empirical evidence shows that most of the proteins secreted in nectar (nectarins) are enzymes that can tailor nectar chemistry for their animal mutualists or reduce the growth of microorganisms in nectar. However, to date, the function of many nectarins remains unknown, and very few plant species have had their nectar proteome thoroughly investigated. Mucuna sempervirens (Fabaceae) is a perennial woody vine native to China. Nectarins from this species were separated using two-dimensional gel electrophoresis, and analyzed using mass spectrometry. A L-gulonolactone oxidase like protein (MsGulLO) was detected. MsGulLO has high similarity to L-gulonolactone oxidase 5 (AtGulLO5) in Arabidopsis thaliana, which was suggested to be involved in the pathway of ascorbate biosynthesis; however both MsGulLO and AtGulLO5 are divergent from animal L-gulonolactone oxidases. MsGulLO is suggested to function in hydrogen peroxide generation in nectar but not in plant ascorbate biosynthesis.
2018-08-16 | PXD010067 | Pride
Project description:Floral Nectaries Many plants secrete a rich floral nectar to entice visitation by insect and avian pollinators. In turn, these pollinators transfer pollen between flowers increasing plant fecundity. The nectary is the floral organ that secretes nectar into the base of the flower. The size and abundance of the ornamental tobacco nectaries (Nicotiana sp.) will permit us to isolate up to several grams of nectaries at each stage to obtain the necessary amounts of RNA for probe preparation. Our primary goals to understand the biochemistry the nectary, so that we can manipulate nectary function to increase pollinator visitation. We have previously conducted an EST study and have identified 13596 cDNAs from three different stages of nectary development (Stage 6, immature, presecretory nectaries; Stage 12, mature nectaries at floral anthesis; and nectaries, 44 hours after fertilization. In our efforts to evaluate the transcriptional program for the Nicotiana nectary we are proposing to evaluate nectary mRNAs by hybridization with the potato microarrays. We have preliminary evidence that wholesale transcriptional reprogramming (60% of the transcriptome) occurs during nectary maturation and again following fertilization. Our goal is to understand these processes at a biochemical level so that we can begin manipulating nectary function to improve nectar quality and quantity thereby increasing the attractiveness of flowers to insect pollinators. Such improvements have the potential to result in increases in insect visitation, seedset, and ultimately yield for insect pollinated crops. We are also making significant efforts to understand the restructuring of the nectary during its lifecycle. Many changes occur during nectary development and the observed transcriptional reprogramming makes sense the when these many changes are accounted for. Keywords: Loop design 30 hybs total
2007-09-01 | E-GEOD-8245 | biostudies-arrayexpress
Project description:The goal of the research is to identify the physiological pathways that influence survival, growth, and competitive ability of the species of yeast that colonize floral nectar. Initially sterile, floral nectar is colonized by multiple species of microbes via insects and birds that visit the flowers for nectar. Once colonized, the microbes face two major challenges of the nectar environment: high osmotic pressure, caused by excessive carbon supply, and strong resource competition, caused by low nitrogen availability. We propose to study the genetic basis of the unique ecological strategies that allow nectar yeasts to cope with these challenges, and to determine the effects that these genes may have on microbe microbe interactions in nectar and the chemical properties of nectar that affect pollinator preference.
The work (proposal:https://doi.org/10.46936/10.25585/60001130) conducted by the U.S. Department of Energy Joint Genome Institute (https://ror.org/04xm1d337), a DOE Office of Science User Facility, is supported by the Office of Science of the U.S. Department of Energy operated under Contract No. DE-AC02-05CH11231.
2023-08-04 | MSV000092600 | MassIVE