Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

The acetylated lysine residues of Acs (TPA&control)

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

ORGANISM(S): Escherichia Coli Bw25113

SUBMITTER: Weihong Jiang

PROVIDER: PXD031674 | iProX | Mon Feb 14 00:00:00 GMT 2022

REPOSITORIES: iProX

ACCESS DATA

Json Xml

Similar Datasets

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 |

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

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 | GSE220919 | GEO

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

2024-03-20 | GSE220918 | GEO

The acetylated lysine residues of AdhE

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

2021-09-08 | PXD028234 |

The acetylated lysine residues of Pta

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

2021-09-08 | PXD028235 |

The acetylated lysine residues in C. ljungdahlii

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

2021-09-08 | PXD028233 |

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

Project description:Role of MYC acetylated lysine residues in cell transformation and gene-selective regulation

| PRJNA911991 | ENA

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

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

| PRJNA912073 | ENA

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

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

| PRJNA912074 | ENA

POWERDERESS and HDA9 interact and promote histone H3 deacetylation at specific lysine residues in Arabidopsis. [RNA-Seq]

Project description:Histone acetylation is a major epigenetic control mechanism that is tightly linked to the promotion of gene expression. Histone acetylation levels are balanced through the opposing activities of histone acetyltransferases (HATs) and histone deacetylases (HDACs). Arabidopsis HDAC genes (AtHDACs) compose a large gene family, and distinct phenotypes among AtHDAC mutants reflect the functional specificity of individual AtHDACs. However, the mechanisms underlying this functional diversity are largely unknown. Here, we show that POWERDRESS (PWR), a positive regulator of floral stem cell maintenance, interacts with HDA9 and promotes histone H3 deacetylation possibly by facilitating HDA9 function at target chromatin. The PWR SANT2 domain, which is homologous to that of subunits in animal HDAC complexes, showed specific binding affinity to acetylated histone H3. Three lysine residues (K9, K14 and K27) of H3 retained hyperacetylation status in both pwr and hda9 mutants. Genome wide H3K9 and H3K14 acetylation levels were generally elevated, and a large portion of acetylated targets overlapped between the pwr and hda9 mutants. Comparative analysis revealed a correlation between gene expression and histone H3 acetylation status in the pwr and hda9 mutants. In addition, PWR and HDA9 modulated the AGAMOUS-LIKE 19 (AGL19)-mediated flowering time pathway through histone H3 deacetylation. Finally, PWR was shown to physically interact with HDA9. We therefore propose that PWR acts as a subunit in a complex with HDA9 to negatively regulate the acetylation of specific lysine residues of histone H3 at genomic targets.

2017-01-25 | GSE89769 | 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