Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

2 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Acetylated sites of C.ljungdahlii in fructose and gas

ABSTRACT: detection the acetylated lysine residues C. ljungdahlii in fructose and gas

ORGANISM(S): Clostridium Ljungdahlii Dsm 13528

SUBMITTER: Weihong Jiang

PROVIDER: PXD029413 | iProX | Thu Oct 28 00:00:00 BST 2021

REPOSITORIES: iProX

ACCESS DATA

Json Xml

Publications

Protein acetylation-mediated cross regulation of acetic acid and ethanol synthesis in the gas-fermenting Clostridium ljungdahlii.

Liu Yanqiang Y Zhang Ziwen Z Jiang Weihong W Gu Yang Y

The Journal of biological chemistry 20211224 2

The autotrophic acetogen Clostridium ljungdahlii has emerged as a major candidate in the biological conversion of one-carbon gases (CO<sub>2</sub>/CO) to bulk chemicals and fuels. Nevertheless, the regulatory pathways and downstream metabolic changes responsible for product formation and distribution in this bacterium remain minimally explored. Protein lysine acetylation (PLA), a prevalent posttranslational modification, controls numerous crucial cellular functions. Herein, we revealed a novel c ...[more]

PMID: 34954142

Similar Datasets

Mapping of H4-acetylated chromatin modifications in differentiating human primary myoblasts

Project description:We assessed the genomic distribution of H4-acetylated chromatin by ChIP using SNP chips and an antibody specific to four acetylated lysine residues of H4. Keywords: Comparative genomic hybridization

2006-08-28 | GSE4132 | GEO

The acetylated lysine residues of Pta

Project description:detection the acetylated lysine residues of Pta (C. ljungdahlii))

2021-09-08 | PXD028235 | iProX

The acetylated lysine residues of AdhE

Project description:detection the acetylated lysine residues of AdhE (C. ljungdahlii))

2021-09-08 | PXD028234 | iProX

The acetylated lysine residues in C. ljungdahlii

Project description:detection the acetylated lysine residues in C. ljungdahlii

2021-09-08 | PXD028233 | iProX

Role of MYC acetylated lysine residues in cell transformation and gene-selective regulation [MCF10A]

Project description:The functions of MYC acetylation have remained unclear. In this study we identified the major lysine residues of MYC that are acetylated by p300 and GCN5 in cancer cell lines and established the requirment of three specific acetyl-lysine (AcK) residues for MYC transformation of Rat1a fibroblasts and MCF10 mammary epithelial cells. We further uncovered gene-selective regulatory functions and conserved genetic programs and biolofical processes regulated by MYC AcK residues in both cell types.

2024-03-20 | GSE220918 | GEO

Role of MYC acetylated lysine residues in cell transformation and gene-selective regulation [Rat1A]

2024-03-20 | GSE220919 | GEO

The acetylated lysine residues of Acs (TPA&control)

Project description:Detection the acetylated lysine residues of Acs (between the TPA editor-mediated acetylation (At2-dCas12a-crRNA) and the true acetylation in vivo (dCas12a-crRNA))

2022-02-14 | PXD031674 | iProX

The acetylated lysine residues of RNase II (TPA&control)

Project description:detection the acetylated lysine residues of RNase II (between the TPA editor-mediated acetylation (At2-dCas12a-crRNA) and the true acetylation in vivo (dCas12a-crRNA))

2022-02-14 | PXD031675 | iProX

Acetyl-methyllysine marks chromatin at active transcription start sites

Project description:Lysine residues in histones and other proteins can be modified by post-translational modifications (PTMs) that encode regulatory information. Acetylation and methylation of histone lysine residues are especially important for regulating chromatin and gene expression. Pathways involving these PTMs are targets for clinically approved therapeutics to treat human diseases. Lysine methylation and acetylation are generally assumed to be mutually exclusive at the same residue. Here, we report the discovery of cellular lysine residues that are both methylated and acetylated on the same sidechain to form acetyl-methyllysine (Kacme). We show that Kacme is found on histone H4 across a range of species and across mammalian tissues. Kacme is associated with marks of active chromatin and is regulated in response to biological signals. Analysis of nascent transcription and promoter-proximal pausing in human cells demonstrates that higher levels of Kacme are associated with higher levels of initiation and transcription. H4Kacme can be installed by enzymatic acetylation of monomethylated lysine peptides and is resistant to deacetylation by some HDACs in vitro. Further, Kacme can be bound by chromatin proteins that recognize modified lysine residues as we demonstrate with the crystal structure of acetyllysine-binding protein BRD2 bound to a histone H4Kacme peptide. These results establish Kacme as a new cellular PTM with the potential to encode information distinct from methylation and acetylation alone and demonstrate that Kacme has all the hallmarks of a PTM with fundamental importance to chromatin biology.

2023-07-21 | GSE182204 | GEO

Site-specifically acetylated G6PD

Project description:Site-specifically acetylated G6PD expressed in bacteria or cultured mammalian cells by genetically encoding the incorporation of acetylated lysine. Purified G6PD (expressed in E. coli) or immunopurified G6PD (expressed in HEK293T cells) were subjected to LC-MS/MS analysis.

2023-10-24 | PXD044906 | Pride

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

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