GNPS - RiPP Metal Binding Assessment at High pH
Ontology highlight
ABSTRACT:
INSTRUMENT(S): QExactive Tandem Mass Spectrometry
ORGANISM(S): None
SUBMITTER: 
Allegra Aron
PROVIDER: MSV000095656 | GNPS | Tue Aug 20 10:37:00 BST 2024
REPOSITORIES: GNPS
Similar Datasets
Project description:Does the RiPP compound bind Cu2+, Cu+, or Fe2+? Assessing to see whether this Novel RiPP compound binds or not since it possesses the properties of methanobactin
2024-08-20 | MSV000095656 | MassIVE
Project description:Microbulbifer RiPP has the ability to bind strongly with Copper even in competitive metal binding experiments
| MSV000095853 | MassIVE
Project description:RiPP has the potential to binding metal. Investigating the type of metal this binds is key
2024-08-14 | MSV000095600 | MassIVE
Project description:RiPP has the potential to binding metal. Investigating the type of metal this binds is key
2024-08-14 | MSV000095600 | GNPS
Project description:Microbulbifer RiPP has the ability to bind strongly with Copper even in competitive metal binding experiments
| MSV000095853 | GNPS
Project description:To determine toxicant specific effects of Ordnance Related Compound (ORC) exposure we performed microarray hybridizations with RNA isolated from Daphnia magna following different ORC exposures at the 1/10 LC50. The gene expression profiles revealed toxicant specific gene expression profiles allowed for the identification of specific biomarkers of exposure. Keywords: ecotoxicogenomic exposure study We exposed Daphnia magna the 1/10 LC50 of different Ordnance Related Compounds (Cu, Zn, Pb, WO4, RDX, TNT, 2-ADNT, 2-ADNT, TNB, DNB, 2,4-DNT, and 2,6-DNT) for 24 hours. For each exposure condition, we performed 3 exposures and 2 technical replicates (as dye swap) for each exposure (6 microarrays total, except TNT and Cu). All exposures were compared to a unexposed laboratory control (MHRW media).
2010-05-18 | E-GEOD-13169 | biostudies-arrayexpress
Project description:MTF1 is a highly conserved metal-binding transcription factor in eukaryotes. MTF1 binds to DNA sequence motifs, termed metal response elements (MREs) to induce the expression of genes involved in metal and oxidative stress homeostasis. MTF1 is responsive to both metal excess and deprivation, and can also protect cells from oxidative and hypoxic stresses. Disruption of metal homeostasis leads to the development of several pathological states. Despite its roles in these processes , MTF1 has been shown to be required for developmental processes such as embryonic liver formation. In this study, we used multiple strategies to understand the mechanism by which MTF1 functions in skeletal muscle differentiation and to determine the role cellular copper (Cu) status plays in this process. We provide the functional relationships between MTF1, Cu, myogenic gene promoters, and MyoD, an specific component of the myogenic transcriptional machinery in differentiating primary myoblasts derived from mouse satellite cells. We found that MTF1 is induced and translocated to the nucleus upon initiation of myogenesis. Consistent with previous studies from our laboratory , addition of non-toxic concentrations of Cu promote myogenesis and enhanced MTF1 expression. CRISPR/Cas9-mediated depletion of MTF1 demonstrated that MTF1 is essential for proper development of skeletal muscle, as partial Mtf1 knockdown leads to apoptosis to differentiating myoblasts. MTF1 was also found to bind Cu at a carboxy-terminal tetra-cysteine cluster, which may contribute to the mobilization of Cu to the nucleus during myogenesis. ChIP-seq and ChIP-qPCR analyses showed that MTF1 binds at the promoter regions of myogenic genes as part of a complex with MyoD, the master transcriptional regulator of the myogenic lineage. These results have the potential to initiate a new area of research in MTF1 function and in the regulation of myogenesis. Furthermore, these studies set the basis to understand the role of Cu at the transcriptional level, affects growth and development and will contribute to the largely unexplored are of muscular phenotypes observed in human pathologies associated to Cu misbalance, such as Menkes’ and Wilson’s diseases.
2019-10-04 | GSE116331 | GEO
Project description:Limited data are available on the impacts of copper (Cu)-pH-interaction-responsive genes in roots. Citrus sinensis seedlings were treated with 300 (Cu-toxicity) or 0.5 uM (control) CuCl2 x pH 3.0 or 4.8 for 17 weeks. Thereafter, we investigated the impacts of Cu-pH interactions on transcriptomics in roots.
2023-02-17 | GSE225124 | GEO
Project description:<p>Increasing studies associating glycerophospholipids with various pathological conditions highlight the need for their thorough characterization. However, the intricate composition of the lipidome due to the presence of lipid isomers poses significant challenges to structural lipidomics. This study uses the anodic corrosion of two metals in a single theta nESI emitter as a tool to simultaneously characterize lipids at multiple isomer levels. Anodic corrosion of cobalt and copper in the positive ion mode generates the metal-adducted lipid complexes, [M+Co]2+ and [M+Cu]+, respectively. Optimization of parameters such as the distances of the electrodes from the nESI tip allowed the achievement of the formation of one metal-adducted lipid product at a time. Collision-induced dissociation (CID) of [M+Co]2+ results in preferential loss of the fatty acyl (FA) chain at the sn-2 position, thus generating singly charged sn-specific fragment ions. Whereas, multistage fragmentation of [M+Cu]+ via CID generated a C=C bond position-specific characteristic ion pattern induced by the π-Cu+ interaction. The feasibility of the method was tested on PC lipid extract from egg yolk to identify lipids on multiple isomer levels. Thus, the application of dual metal anodic corrosion allows lipid isomer identification with reduced sample preparation time, no signal suppression by counter anions, low sample consumption and no need for an extra apparatus.</p>
2023-10-10 | MTBLS8547 | MetaboLights
Project description:Enzymes that generate ribosomally synthesized and posttranslationally modified peptide (RiPP) natural products have garnered significant interest, given their ability to produce large libraries of chemically diverse scaffolds. Such RiPP biosynthetic enzymes are predicted to bind their corresponding peptide substrates through sequence-specific recognition of the leader sequence, which is removed after the installation of posttranslational modifications on the core sequence. The conservation of the leader sequence within a given RiPP class, in otherwise disparate precursor peptides, further supports the notion that strict sequence specificity is necessary for leader peptide engagement. Here, we demonstrate that leader binding by a biosynthetic enzyme in the lasso peptide class of RiPPs is directed by a minimal number of hydrophobic interactions. Biochemical and structural data illustrate how a single leader-binding domain can engage sequence-divergent leader peptides using a conserved motif that facilitates hydrophobic packing. The presence of this simple motif in noncognate peptides results in low micromolar affinity binding by binding domains from several different lasso biosynthetic systems. We also demonstrate that these observations likely extend to other RiPP biosynthetic classes. The portability of the binding motif opens avenues for the engineering of semisynthetic hybrid RiPP products.
| S-EPMC6883790 | biostudies-literature