Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

The large GTPase AtGBPL3 links nuclear envelope formation to lamina-associated gene silencing [RNA-seq]

ABSTRACT: Guanylate Binding Proteins (GBPs) are prominent regulators of immunity unknown to be required for nuclear envelope formation and function. The Arabidopsis GBP orthologue AtGBPL3 was identified as a novel component of the plant lamina, with essential functions in mitotic nuclear envelope reformation. AtGBPL3 is preferentially expressed in mitotically active root tips, accumulates at the nuclear envelope and interacts with further components of the nuclear lamina. To investigate effects of defective lamina components on gene expression, we analysed the transcriptomes of 4 day old wild-type, gbpl3-5, crwn4-1, crwn1-1crwn4-1, as well as gbpl3-5 mutants expressing GBPL3-GFP or the GTPase-dead GBPL3(K83A)-GFP under control of the AtGBPL3-promoter.

ORGANISM(S): Arabidopsis thaliana

PROVIDER: GSE221661 | GEO | 2022/12/23

REPOSITORIES: GEO

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Similar Datasets

The large GTPase AtGBPL3 links nuclear envelope formation to lamina-associated gene silencing [ChIP-Seq]

Project description:Guanylate Binding Proteins (GBPs) are prominent regulators of immunity unknown to be required for nuclear envelope formation and function. The Arabidopsis GBP orthologue AtGBPL3 was identified as a novel component of the plant lamina, with essential functions in mitotic nuclear envelope reformation. AtGBPL3 is preferentially expressed in mitotically active root tips and accumulates at the nuclear envelope. Furthermore, fluorescent lifetime imaging experiments in the presence or absence of the chromatin-labelling dye Sytox-Orange suggested that GBPL3 might be able to interact with chromatin. Chromatin-immunoprecipitation followed by sequencing (ChIP-Seq) revealed only few GBPL3-associated chromatin domains, which were concentrated particularly within or near centromeric regions.

2022-12-23 | GSE221668 | GEO

Inducible repositioning of mouse gene tethering to the inner nuclear membrane

Project description:Nuclear compartmentalization appears to play an important role in regulating metazoan genes. While studies on immunoglobulin (Ig) and other loci have correlated positioning at the nuclear lamina with gene repression, the functional consequences of this compartmentalization remain untested. We devised an approach for inducible tethering of genes to the inner nuclear membrane (INM) and demonstrate with 3D DNA-ImmunoFISH, repositioning of chromosomal regions to the nuclear lamina. Relocalization requires mitotic nuclear envelope breakdown and reformation. Tethering leads to the accumulation of lamin and INM proteins but not to association with pericentromeric heterochromatin or nuclear pore complexes. Recruitment of genes to the INM can result in their transcriptional repression. Using DamID we show that as is the case for our model system, inactive Ig loci at the nuclear periphery are contacted by INM and lamina components. We propose that such molecular interactions are used to compartmentalize and limit the accessibility of Ig loci. Experiment Overall Design: We used microarray to analyze the transcription status of genomic regions are inducibly tethered to the INM

2008-06-11 | E-GEOD-10176 | biostudies-arrayexpress

Inducible repositioning of genes to the inner nuclear membrane

2008-01-16 | GSE10176 | GEO

CRWN nuclear lamina components maintain the H3K27me3 landscape and promote successful reproduction in Arabidopsis

Project description:The nuclear lamina, a crucial sub-nuclear protein matrix, maintains nuclear structure and genomic function. Our study centers on the Arabidopsis lamina component CROWDED NUCLEIs (CRWNs), unveiling their extensive role in the development of the reproductive system with a specific focus on the endosperm, which is pivotal in seed development. We showed that quadruple crwn null gametophytes exhibit limited viability, and crwn1 crwn2 (crwn1/2) mutations lead to defective seeds often having enlarged chalazal cysts and variable timing of endosperm cellularization. crwn1/2 endosperm also exhibit perturbations of level of tri-methylation of lysin 27 on histone H3 (H3K27me3) and transcriptomics. In addition, we found that PHERES1 (PHE1) targets and defense-related genes are mis-regulated in crwn1/2 endosperm, showing that both development and stress responses are affected by CRWNs simultaneously. The data also suggest that CRWNs affect various aspects of physiology of both vegetative and reproductive tissues but there are tissue-specific roles.

2024-05-02 | GSE243032 | GEO

The large GTPase AtGBPL3 links nuclear envelope formation to lamina-associated gene silencing

Project description:The large GTPase AtGBPL3 links nuclear envelope formation to lamina-associated gene silencing

| PRJNA915350 | ENA

The large GTPase AtGBPL3 links nuclear envelope formation to lamina-associated gene silencing [ChIP-Seq]

Project description:The large GTPase AtGBPL3 links nuclear envelope formation to lamina-associated gene silencing [ChIP-Seq]

| PRJNA915355 | ENA

The large GTPase AtGBPL3 links nuclear envelope formation to lamina-associated gene silencing [RNA-seq]

Project description:The large GTPase AtGBPL3 links nuclear envelope formation to lamina-associated gene silencing [RNA-seq]

| PRJNA915344 | ENA

Effect of truncation mutants of the trypanosomatid nuclear lamina protein NUP-1 on the whole cell proteome in T. brucei

Project description:The nuclear lamina has multiple functions, including maintaining nuclear structural integrity and differential gene expression. Correct spatial and temporal lamina assembly is essential to meet these and other roles. Recently, it emerged that multiple lamina systems exist that are likely products of independent origins, while all these systems share remarkably analogous functions. Several lamina proteins are known in trypanosomes, two of which, NUP-1 and NUP-2, are essential, coiled-coil proteins with a molecular mass 450 and 250 kDa, respectively. Sequence analysis indicates distinct quaternary structures when compared to the ~60 kDa lamin proteins of multiple lineages, including metazoa. To uncover organisational principles of the trypanosome lamina we generated NUP-1 deletion mutants (N=N-terminal domain; C= C-terminal domain; NC: fusion of the N- and C-terminal domain with entire repeat region deletedd))designed to identify domains of NUP-1 responsible for oligomerisation. We find that both N- and C-termini act as interaction domains and disruption of these interactions impacts additional components of the lamina, the nuclear envelope and nucleoporin TbNup98. By contrast there is remarkably little impact on transcription, crucially including silencing of telomeric variant surface glycoprotein genes. These data indicate that both terminal domains of NUP-1 have roles in assembling the trypanosome lamina and suggest an architecture distinct to the lamin system is based on a ‘hub and spoke’ configuration.

2021-06-03 | PXD019978 | Pride

Genome-wide maps of nuclear lamina interactions in HeLa cells identified using MethylAdenine IDentification (MadID).

Project description:Mapping of lamina-associated domains using MadID experiment. A methyltransferase (M.EcoGII) targeted to the nuclear envelope is able to add methyl groups to adenine residues (m6A) on chromatin in contact to the nuclear periphery. A m6A-specific immunoprecipitation is performed on isolated genomic DNA, followed by Ilumina deep sequencing to identify contact sites.

2018-10-26 | E-MTAB-6888 | biostudies-arrayexpress

Identification of PP2A-B55 targets in Drosophila uncovers regulation of Emerin during nuclear envelope reassembly

Project description:Entry into mitosis is triggered by mitotic kinases that phosphorylate multiple proteins to induce profound cellular changes including nuclear envelope breakdown, chromosome condensation and spindle assembly. Conversely, mitotic exit requires protein dephosphorylation as cells return to their interphase organization. Protein Phosphatase 2A in complex with its B55/Tws regulatory subunit (PP2A-B55) is known to play a crucial role in this transition. However, the precise events and substrates that it regulates are incompletely understood. We used proteomic approaches in Drosophila to identify proteins that interact with PP2A-B55 and are dephosphorylated in a PP2A-B55 dependent manner. Among several candidates, we identified Otefin (also known as Emerin) as a target of PP2A-B55 in the process of nuclear envelope reformation after mitosis. Emerin is a protein of the inner nuclear membrane that interacts with the DNA-binding protein Barrier-to-Autointegration Factor (BAF) via a LEM domain. Our results indicate that phosphorylation of Emerin at Ser50 and Ser54 near its LEM domain negatively regulates its association with BAF, Lamin and additional Emerin. Using live imaging, we show that dephosphorylation of Emerin at the identified sites determines the timing of nuclear envelope reformation. Genetic rescue experiments indicate that this regulation is required in vivo during embryonic development. Phosphoregulation of the Emerin-BAF complex formation by PP2A-B55 appears as a key event of mitotic exit that is likely to be conserved across species.

2023-08-10 | PXD041030 | Pride

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