Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Tequatrovirus T4

ABSTRACT: Autoinhibition of a clamp-loader ATPase revealed by deep mutagenesis and cryo-EM

PROVIDER: PRJNA1025274 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR26348600_1.fastq.gz	Fastqsanger.gz
	SRR26348600_2.fastq.gz	Fastqsanger.gz
	SRR26348601_1.fastq.gz	Fastqsanger.gz
	SRR26348601_2.fastq.gz	Fastqsanger.gz
	SRR26348602_1.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 76

Similar Datasets

Tequatrovirus T4

Project description:Chin et al_Bacteriophage T4_Raw sequence reads

| PRJNA737295 | ENA

Tequatrovirus T4

Project description:Microarray Analysis of Gene Expression during Bacteriophage T4 Infection

| PRJNA93685 | ENA

Tequatrovirus T4

Project description:Tequatrovirus T4 Raw sequence reads

| PRJNA1076877 | ENA

Tequatrovirus T4

Project description:CRISPR/Cas engineered Escherichia virus T4 long-read amplicon raw sequence reads

| PRJNA952186 | ENA

Project description:Cryo-EM of the Saccharolobus solfataricus POZ149 pilus

| PRJNA616127 | ENA

A Structure-Based Mechanism for DNA Entry into the Cohesin Ring

Project description:The ring-shaped cohesin complex is thought to fulfil its roles in sister chromatid cohesion, genome stability and gene regulation by topologically encircling DNAs. The ring is formed by two Structural Maintenance of Chromosome (SMC) subunits, whose ATPase heads are linked by a kleisin subunit. Additional components, including the Mis4Scc2/NIPL cohesin loader, engage the kleisin. Here, we visualize a DNA gripping intermediate during cohesin loading onto DNA by cryo-electron microscopy. ATP-dependent head engagement creates an interaction surface onto which Mis4Scc2/NIPL clamps the DNA. We use biophysical tools to establish the order of events during cohesin loading. DNA first traverses an N-terminal kleisin gate that was opened by ATP binding and closed again as the loader locks the DNA. Ensuing ATP hydrolysis and head disengagement, assisted by Mis4Scc2/NIPL, will complete DNA entry. A conserved kleisin N-terminal tail guides the DNA on its trajectory to successful topological DNA entry into the cohesin ring.

2020-08-05 | PXD018600 | Pride

Functional crosstalk between the cohesin loader and a chromatin remodeler

Project description:The Scc2-Scc4 complex interacts with a conserved RSC ATPase motor module. The cohesin loader enhances RSC remodeling activity in vitro and promoter nucleosome eviction in vivo.

2022-03-01 | GSE197657 | GEO

Functional crosstalk between the cohesin loader and chromatin remodelers

Project description:The cohesin complex has crucial roles in many structural and functional aspects of chromosomes including sister chromatid cohesion, genome organization, gene transcription and DNA repair. Cohesin recruitment onto chromosomes requires nucleosome free DNA and a specialized cohesin loader complex comprised of the Scc2 and Scc4 subunits. The cohesin loader, in addition to stimulating cohesin ATP hydrolysis and facilitating topological loading onto DNA, leads cohesin to chromatin receptors such as the RSC chromatin remodeling complex. Here, we explore the cohesin loader-RSC interaction and show that its Scc4 subunit contacts a conserved RSC ATPase motor module. The cohesin loader enhances RSC chromatin remodeling activity in vitro, as well as promoter nucleosome eviction in vivo. These findings provide insight into how the cohesin loader recognizes, as well as influences, the chromatin landscape, with implications for our understanding of human developmental disorders including Cornelia de Lange and Coffin-Siris syndromes.

2022-11-29 | PXD033446 | Pride

Structural basis of MICAL autoinhibition

Project description:MICAL proteins play a crucial role in cellular dynamics by binding and disassembling actin filaments, impacting processes like axon guidance, cytokinesis, and cell morphology. Their cellular activity is tightly controlled, as dysregulation can lead to detrimental effects on cellular morphology. Although previous studies have suggested that MICALs are autoinhibited, and require Rab proteins to become active, the detailed molecular mechanisms remained unclear. Here, we report the cryo-EM structure of human MICAL1 at a nominal resolution of 3.1 Å. Structural analyses, alongside biochemical and functional studies, show that MICAL1 autoinhibition is mediated by an intramolecular interaction between its N-terminal catalytic and C-terminal coiled-coil domains, blocking F-actin interaction. Moreover, we demonstrate that allosteric changes in the coiled-coil domain and the binding of the tripartite assembly of CH-L2α1-LIM domains to the coiled-coil domain are crucial for MICAL activation and autoinhibition. These mechanisms appear to be evolutionarily conserved, suggesting a potential universality across the MICAL family.

2024-10-30 | PXD057312 | Pride

Genomic analysis of replication profiles identifies RFCCtf18 as a key mediator of the replication stress response

Project description:Maintenance of genome stability during DNA replication depends on surveillance mechanisms that prevent fork collapse and regulate replication timing. To dissect the checkpoint pathways signalling paused forks, we have screened a collection of S. cerevisiae mutants for their ability to activate Rad53, using the repression of late origins as readout for checkpoint efficiency. These genomic data redefine the role of key checkpoint factors. Indeed, they show that DNA damage sensors such as the 9-1-1 clamp and its loader RFCRad24 are unexpectedly dispensable to signal paused forks. In contrast, we found that the alternative clamp loader RFCCtf18 is essential for the Mrc1-dependent activation of Rad53. Moreover, we report that forks collapse in ctf18delta mutants and activate a secondary checkpoint pathway that represses very late origins in a Rad9-dependent manner. We propose a novel and integrated view of the replication checkpoint in which different pathways cooperate to fine tune the cellular response to arrested forks.

2010-10-26 | GSE21014 | 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