Anthraquinone regulation in P. luminescens
Ontology highlight
ABSTRACT:
PROVIDER: PRJEB16309 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| ERR1697130.fastq.gz | Fastqsanger.gz | |||
| ERR1697131.fastq.gz | Fastqsanger.gz | |||
| ERR1697132.fastq.gz | Fastqsanger.gz | |||
| ERR1697125.fastq.gz | Fastqsanger.gz | |||
| ERR1697126.fastq.gz | Fastqsanger.gz |
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Project description:Henry2016 Folate pathway model with induced
PanB reaction
This model is described in the article:
Experimental and Metabolic
Modeling Evidence for a Folate-Cleaving Side-Activity of
Ketopantoate Hydroxymethyltransferase (PanB).
Thiaville JJ, Frelin O,
García-Salinas C, Harrison K, Hasnain G, Horenstein NA,
Díaz de la Garza RI, Henry CS, Hanson AD, de
Crécy-Lagard V.
Front Microbiol 2016; 7: 431
Abstract:
Tetrahydrofolate (THF) and its one-carbon derivatives,
collectively termed folates, are essential cofactors, but are
inherently unstable. While it is clear that chemical oxidation
can cleave folates or damage their pterin precursors, very
little is known about enzymatic damage to these molecules or
about whether the folate biosynthesis pathway responds
adaptively to damage to its end-products. The presence of a
duplication of the gene encoding the folate biosynthesis enzyme
6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (FolK) in
many sequenced bacterial genomes combined with a strong
chromosomal clustering of the folK gene with panB, encoding the
5,10-methylene-THF-dependent enzyme ketopantoate
hydroxymethyltransferase, led us to infer that PanB has a side
activity that cleaves 5,10-methylene-THF, yielding a pterin
product that is recycled by FolK. Genetic and metabolic
analyses of Escherichia coli strains showed that overexpression
of PanB leads to accumulation of the likely folate cleavage
product 6-hydroxymethylpterin and other pterins in cells and
medium, and-unexpectedly-to a 46% increase in total folate
content. In silico modeling of the folate biosynthesis pathway
showed that these observations are consistent with the in vivo
cleavage of 5,10-methylene-THF by a side-activity of PanB, with
FolK-mediated recycling of the pterin cleavage product, and
with regulation of folate biosynthesis by folates or their
damage products.
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2024-09-02 | BIOMD0000000690 | BioModels
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2024-12-10 | GSE280936 | GEO
Project description:Alas2 gene encodes the rate-limiting enzyme in heme biosynthesis. CRISPR/Cas9-mediated ablation of two Alas2 intronic cis-elements strongly reduced GATA-1-induced Alas2 transcription, heme biosynthesis, and GATA-1 regulation of other vital constituents of the erythroid cell transcriptome. Bypassing Alas2 function in Alas2 cis-element-mutant (double mutant) cells by providing its catalytic product 5-aminolevulinic acid (5-ALA) rescued heme biosynthesis and the GATA-1-dependent genetic network. We discovered a GATA factor- and heme-dependent circuit that establishes the erythroid cell transcriptome. G1E-ER-GATA-1 WT and double mutant cells were examined. Untreated WT, beta-estradiol-treated WT, beta-estradiol-treated double-mutant, and beta-estradiol/5-ALA-treated double-mutant cells were subjected to RNA-seq.
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