Rhizosphere metagenomic library
Ontology highlight
ABSTRACT:
PROVIDER: PRJEB31386 | ENA |
REPOSITORIES: ENA
Similar Datasets
Project description:Plants endo-beta-1,4-glucanases, belonging to Glycoside Hydrolase Family 9, have functional roles in cell wall biosynthesis and remodeling via endohydrolysis of (1-4)-beta-D-glucosidic linkages. Modification of cell wall chemistry via RNAi-mediated downregulation of PdKOR1, a endo-beta-1,4-glucanase gene, in Populus deltoides, has been shown to have functional consequences to the composition of secondary metabolome and ability of modified roots to interact with microbes. The molecular remodeling that underlies the observable differences at metabolic, physiological and morphological levels in roots is not well understood. Here we used a LC-MS/MS-based proteome profiling approach to survey the molecular remodeling in root tissues of PdKOR and control plants. A total of 14316 peptides were identified and these mapped to 7139 P. deltoides. Based on 90% sequence identity, the measured protein accessions represent 1187 functional protein groups. Analysis of GO categories and specific individual proteins shows differential expression of proteins relevant to plant-microbe interactions, cell wall chemistry and metabolism. This proteome dataset can serve as a useful resource for deriving new hypotheses and empirical testing pertaining to functional roles of proteins and pathways in differential priming of plant roots to interactions with microbes.
2020-03-06 | MSV000085068 | MassIVE
Project description:Cellulases and related β-1,4-glucanases are essential components of lignocellulose-degrading enzyme mixtures. The detection of β-1,4-glucanase activity typically relies on monitoring the breakdown of purified lignocellulose-derived substrates or synthetic chromogenic substrates, limiting the activities which can be detected and complicating the tracing of activity back to specific components within complex enzyme mixtures. As a tool for the rapid detection and identification of β-1,4-glucanases, a series of glycosylated cyclophellitol inhibitors mimicking β-1,4-glucan oligosaccharides have been synthesised. These compounds are highly efficient inhibitors of HiCel7B, a well-known GH7 endo-β-1,4-glucanase. An elaborated activity-based probe facilitated the direct detection of β-1,4-glucanases within a complex fungal secretome without any detectable cross-reactivity with β-D-glucosidases. These probes and inhibitors add valuable new capacity to the growing toolbox of cyclophellitol-derived probes for the activity-based profiling of biomass-degrading enzymes.
2021-09-09 | PXD019930 | Pride
Project description:Characterization of a metagenomic regulatory sequence library derived from M. xanthus, E. coli, and O. urethralis genomes in strains expressing different RpoD ortholog variants. Targeted DNA and RNA seq used to profile relative DNA and RNA abundances, respectively of each regulatory sequence construct in the library.
2022-06-07 | E-MTAB-9111 | biostudies-arrayexpress
Project description:We examined the effect of high-level expression of the commercially important endo-1,4-β-xylanase XynA on the B. subtilis transcriptome using RNA-seq. Rather unexpectedly, we found a reduced expression of several protein chaperones, including ClpC, ClpE and ClpX, was downregulated when XynA was overproduced. Expression of these proteins is controlled by the transcriptional repressor CtsR. CtsR levels are directly controlled by regulated proteolysis, involving ClpC and its cognate protease ClpP. Preventing this downregulation by knocking out the involved transcriptional repressor CtsR resulted in increased XynA production by more than 25 %.
2023-02-21 | GSE217916 | GEO
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