Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

GNPS - Priestia endophytica fluorescent pigments

ABSTRACT: The endophytic bacterium Priestia endophytica (Bacillus endophyticus) UCM B-5715 (= DSM 13796) has been found to produce a distinctive pink pigment exhibiting vibrant yellow fluorescence. Investigation of the pigment extract revealed the presence of 2 non-polar fluorescent-colored compounds, with molecular masses of 376 (14.12%) and 410 (82.02%) a.m.u. FTIR spectroscopy indicated the characteristic signatures of heliomycin and chlorxanthomycin IR spectra, respectively. The chlorxathomycin nature of the main compound was confirmed by H1 NMR spectroscopy. Light, luminescence, and transmission electron microscopy, as well as IR and H1 NMR spectroscopy, established a close association between the colored fluorescent compounds and poly-beta-hydroxybutyrate granules. Genome analysis utilizing the antiSMASH 6.0 tool unveiled key gene sequences encoding the type II polyketide synthase complex and halogenase, involved in the biosynthesis of heliomycin and chlorxanthomycin. Given the similarity of chlorxanthomycin to heliomycin, a well-known antimicrobial, and antitumor antibiotic, this pigment might share similar properties with the potential for medical application.

INSTRUMENT(S): Agilent 6890N/5973inert, 1200 series LC/MSD SL

ORGANISM(S): Bacillus Endophyticus (ncbitaxon:135735)

SUBMITTER: Alina Kharchuk

PROVIDER: MSV000093092 | GNPS | Thu Oct 12 22:21:00 BST 2023

REPOSITORIES: GNPS

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Similar Datasets

Priestia endophytica fluorescent pigments

Project description:The endophytic bacterium Priestia endophytica (Bacillus endophyticus) UCM B-5715 (= DSM 13796) has been found to produce a distinctive pink pigment exhibiting vibrant yellow fluorescence. Investigation of the pigment extract revealed the presence of 2 non-polar fluorescent-colored compounds, with molecular masses of 376 (14.12%) and 410 (82.02%) a.m.u. FTIR spectroscopy indicated the characteristic signatures of heliomycin and chlorxanthomycin IR spectra, respectively. The chlorxathomycin nature of the main compound was confirmed by H1 NMR spectroscopy. Light, luminescence, and transmission electron microscopy, as well as IR and H1 NMR spectroscopy, established a close association between the colored fluorescent compounds and poly-beta-hydroxybutyrate granules. Genome analysis utilizing the antiSMASH 6.0 tool unveiled key gene sequences encoding the type II polyketide synthase complex and halogenase, involved in the biosynthesis of heliomycin and chlorxanthomycin. Given the similarity of chlorxanthomycin to heliomycin, a well-known antimicrobial, and antitumor antibiotic, this pigment might share similar properties with the potential for medical application.

2023-10-12 | MSV000093092 | MassIVE

Unravelling the mechanism of neurotensin recognition by neurotensin receptor 1

Project description:The conformational ensembles of G-protein coupled receptors (GPCRs) include inactive and active states. Spectroscopy techniques, including NMR, show that agonists, antagonists and other ligands shift the ensemble toward specific states depending on the pharmacological efficacy of the ligand. How receptors recognize ligands and the kinetic mechanism underlying this population shift is poorly understood. Here, we investigate the kinetic mechanism of neurotensin recognition by neurotensin receptor 1 (NTS1) using 19F-NMR, hydrogen-deuterium exchange mass spectrometry and stopped-flow fluorescence spectroscopy. Our results indicate slow-exchanging conformational heterogeneity on the extracellular surface of ligand-bound NTS1. Numerical analysis of the kinetic data of neurotensin binding to NTS1 shows that ligand recognition follows an induced fit mechanism, in which conformational changes occur after neurotensin binding. This approach is applicable to other GPCRs to provide insight into the kinetic regulation of ligand recognition by GPCRs.

2023-12-09 | PXD045464 | Pride

Expression data from zebrafish pigment cells at adult stage

Project description:In zebrafish, there are interactions between black pigment cells (melanophores) and yellow pigment cells (xanthophores) for pigment-pattern formation. However, the detailed molecular mechanism of these interactions remains largely unknown. We used microarray for identifying the molecular basis of these interactions by comparing gene expression between melanophores and xanthophores.

2013-05-30 | GSE42129 | GEO

Expression data from zebrafish pigment cells at adult stage

2013-05-30 | E-GEOD-42129 | biostudies-arrayexpress

Neopetrotaurines A-C, Isoquinoline Alkaloids with an Unprecedented Taurine-Bridged Isoquinoline Quinone Moiety from the Sponge Neopetrosia sp.

Project description:Neopetrotaurines A-C, isoquinoline quinone-linked isoquinoline alkaloids that possess a unique taurine bridge connecting the two bicyclic components, were isolated from a Neopetrosia sp. marine sponge. These new compounds have proton-deficient scaffolds, so their structure elucidation was facilitated by utilizing LR-HSQMBC and HMBC NMR experiments optimized to detect 4- and 5-bond long-range 1H-13C heteronuclear correlations. Neopetrotaurines A-C showed potent inhibition of transcription driven by the oncogenic fusion protein PAX3-FOXO1 in alveolar rhabdomyosarcoma.

2024-03-21 | GSE249431 | GEO

Structural basis for heme-dependent NCoR binding to the transcriptional repressor REV-ERBβ

Project description:Heme is the endogenous ligand for the constitutively repressive REV-ERB nuclear receptors, REV-ERBα (NR1D1) and REV-ERBβ (NR1D2), but how heme regulates REV-ERB activity remains unclear. While cellular studies indicate heme is required for the REV-ERBs to bind the corepressor NCoR and repress transcription, fluorescence-based biochemical assays and crystal structures suggest that heme displaces NCoR. Here, we found that heme artifactually influences detection of NCoR interaction in fluorescence-based assays. Using fluorescence-independent methods, including isothermal titration calorimetry, NMR spectroscopy, and XL-MS, we determined that heme remodels the thermodynamic profile of NCoR binding to REV-ERBβ ligand-binding domain (LBD) and directly increases LBD binding affinity for an NCoR interaction motif. We further report two crystal structures of REV-ERBβ LBD cobound to heme and NCoR peptides, which reveal the heme-dependent NCoR binding mode. By resolving previous contradictory biochemical, structural, and cellular studies, our findings should facilitate renewed progress toward understanding heme-dependent REV-ERB activity.

2021-02-24 | PXD021761 | Pride

Bovine nose tissues: Yellow nose vs. Black nose

Project description:The coat color of mammals is determined by the melanogenesis pathway, which is responsible for maintaining the balance between black-brown eumelanin and yellow-reddish phaeomelanin. It is also believed that the color of the bovine nose is regulated in a similar manner; however, the molecular mechanism underlying pigment deposition in the black nose has yet to be elucidated. The aim of the present study was to identify melanogenesis-associated genes that are differentially expressed in the black vs. yellow nose of native Korean cows. Experiment, Yellow nose vs. Black nose HanWoo

2013-12-26 | E-GEOD-53657 | biostudies-arrayexpress

Linking soil microbial community traits to the soil storage potential of dissolved organic carbon from surface plant litter

Project description:Using Fourier transform ion cyclotron resonance mass spectrometry (FTICR-MS) on microcosm samples from early phase plant litter degradation, we found that proteins and condensed hydrocarbons are the compounds with the strongest correlation to dissolved organic carbon (DOC) concentration. Proteins correlated positively with DOC concentration, while tannins and condensed hydrocarbons correlated negatively with DOC. With nuclear magnetic resonance (NMR) spectroscopy, we identified 15 individual compounds associated with DOC concentration. Through random forest, neural network, and indicator species analyses, we identified bacterial and fungal taxa associated with DOC concentration and additionally identified connections between microorganisms and DOC chemical composition.

| MSV000088109 | MassIVE

Regulation of dynamic pigment cell states at single-cell resolution

Project description:Pigment cells bear molecules with diverse physiological roles across phylogeny and are often under strict evolutionary selection. Thus, the mechanisms of regulating these cells, and the pigments within them, are of critical importance. Here, we explore the regulation of pigment cells in the purple sea urchin Strongylocentrotus purpuratus, an emerging model for understudied pigments at a molecular level. Sea urchins display a variety of pigments in both embryos and adults, but how the pigment cells form during development has not been resolved, nor has their breadth of biological significance been revealed. Known genes expressed by embryonic pigment cells are the transcriptional factor glial cells missing (gcm), and the enzymes pks1 and fmo1,2 and 3 (polyketide synthase1, flavin-dependent monooxygenase 1, 2, 3 respectively). In this study, we took advantage of single cell RNA-seq technology to interrogate the cell state of emerging pigment cells, and to test their diversity in fate and function.

2020-07-31 | GSE155427 | GEO

Absolute quantification of cohesin, CTCF and their regulators in human cells

Project description:We have measured absolute copy numbers and dynamics of cohesin, CTCF and their regulators NIPBL, WAPL and sororin by mass spectrometry, fluorescence-correlation spectroscopy and fluorescence recovery after photobleaching in HeLa cells before and after DNA replication. Comparison of these numbers with chromatin immunoprecipitation-sequencing data implies that some genomic cohesin and CTCF enrichment sites are unoccupied in single cells at any one time.

2019-11-21 | GSE126990 | GEO

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data