Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

MftG is crucial for alcohol metabolism of mycobacteria by linking mycofactocin oxidation to respiration

ABSTRACT: MftG is crucial for alcohol metabolism of mycobacteria by linking mycofactocin oxidation to respiration

PROVIDER: PRJNA1053775 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR27237048_1.fastq.gz	Fastqsanger.gz
	SRR27237048_2.fastq.gz	Fastqsanger.gz
	SRR27237049_1.fastq.gz	Fastqsanger.gz
	SRR27237049_2.fastq.gz	Fastqsanger.gz
	SRR27237050_1.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 24

Similar Datasets

MftG is crucial for alcohol metabolism of mycobacteria by linking mycofactocin oxidation to respiration

Project description:Mycofactocin is a redox cofactor essential for the alcohol metabolism of Mycobacteria. While the biosynthesis of mycofactocin is well established, the mftG gene, which encodes an oxidoreductase of the glucose-methanol-choline superfamily remained functionally uncharacterized. Here, we show that MftG enzymes strictly require mft biosynthetic genes, and are found in 75% of organisms harboring these genes. Gene deletion experiments in Mycolicibacterium smegmatis demonstrated a growth defect of the ∆mftG mutant on ethanol as a carbon source, accompanied by an arrest of cell division reminiscent of mild starvation. Investigation of carbon and cofactor metabolism implied a defect in mycofactocin re-oxidation. Cell-free enzyme assays and respirometry using isolated cell membranes indicated that MftG acts as a mycofactocin dehydrogenase shuttling electrons toward the respiratory chain. Transcriptomics studies also indicated remodeling of redox metabolism to compensate for a shortage of redox equivalents. In conclusion, this work closes an important knowledge gap concerning the mycofactocin system and adds a new pathway to the intricate web of redox reactions governing the metabolism of mycobacteria.

2024-03-01 | GSE250373 | GEO

Nontuberculous mycobacteria

Project description:Nontuberculous mycobacteria Metagenome

| PRJNA779755 | ENA

nontuberculosis mycobacteria

Project description:nontuberculosis mycobacteria Raw sequence reads

| PRJNA974445 | ENA

Mycobacteria species

Project description:Mycobacteria species Raw sequence reads

| PRJNA401515 | ENA

Mycobacteria

Project description:Complete genome sequence of environmental Mycobacteria isolated from water

| PRJNA767558 | ENA

Two faces of an essential PknB substrate in mycobacteria

Project description:Tuberculosis claims nearly 2 million lives annually and its causative agent Mycobacterium tuberculosis is a highly successful pathogen which explores multiple signalling mechanisms to grow and survive in humans for decades. Well-studied protein kinase B (PknB), one of the 11 serine/threonine kinases present in M. tuberculosis, is critical for growth in vitro and in vivo. Here we demonstrate that PknB-depleted mycobacteria can normally replicate and synthesise peptidoglycan in osmoprotective medium. Comparative phosphoproteomics of PknB-producing and PknB-depleted mycobacteria identifies CwlM as a major PknB substrate. Complementation studies of cwlM mutant further support CwlM phosphorylation as the molecular basis for the PknB essentiality. We demonstrate that in growing mycobacteria CwlM is produced in two forms with distinct functions which are essential for growth: a non-phosphorylated membrane-associated CwlM and a PknB-phosphorylated cytoplasmic CwlM. Immunoprecipitation and mycobacterial two hybrid assays reveal partner proteins for phosphorylated and non-phosphorylated CwlM forms, as FhaA, a forkhead-associated domain protein, and MurJ (MviN), a predicted Lipid II flippase, respectively. We propose that PknB is not required for mycobacterial division but coordinates peptidoglycan polymerization and cross-linking by a novel CwlM-mediated mechanism

2018-09-24 | PXD009239 | Pride

Experimental selection of long-term intracellular mycobacteria

Project description:Some intracellular bacteria are known to cause long-term infections for periods of time that last decades without compromising the viability of the host. Although of critical importance, the changes that intracellular bacteria suffer during this long process of residence in a host cell environment remain obscure. Here, we report an experimental approach to study the adaptations of intracellular mycobacteria forced by a long-term intracellular lifestyle. Long-term infection of host macrophages with mycobacteria was maintained for a period of years. Mycobacteria in the long-term infected macrophages underwent an adaptation process leading to impaired phenolic glycolipids (PGL) synthesis, preference for glucose as a carbon source and neutral lipids accumulation. These changes correlated with increased survival of mycobacteria in macrophages and mice during re-infection and specific expression of stress- and survival-related genes. Our findings identify bacterial traits implicated in the establishment of long-term cellular infections and represent a tool for understanding the physiological states of bacteria living in fluctuating intracellular environments.

2014-12-31 | GSE49976 | GEO

Nontubercular Mycobacteria

Project description:Genomes of previously unsequenced Nontubercular Mycobacteria genome sequencing

| PRJNA299467 | ENA

WAS enhance organohalides respiration

Project description:WAS enhance organohalides respiration

| PRJEB40323 | ENA

Human Natural Killer Cell activation by mycobacteria

Project description:Purified NK cells were co-cultured with M. bovis BCG or M. tuberculosis H37Rv (1:1) in the presence of IL-2 (100U/ml) or IL-12 (10pg/ml) for 24h before trizol extraction. We used microarrays to detail the global gene expression underlying NK cell activation by mycobacteria. NK cell were isolated from the blood of 6 independent donors and activated with different mycobacteria and cytokines in order to study their transcriptional profiles according to mycobacterial virulence.

2011-07-26 | E-GEOD-30950 | biostudies-arrayexpress

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