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Actin R256 mono-methylation is a conserved post-translational modification involved in transcription

ABSTRACT: Actin R256 mono-methylation is a conserved post-translational modification involved in transcription

PROVIDER: PRJNA659255 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR12513346_1.fastq.gz	Fastqsanger.gz
	SRR12513346_2.fastq.gz	Fastqsanger.gz
	SRR12513347_1.fastq.gz	Fastqsanger.gz
	SRR12513347_2.fastq.gz	Fastqsanger.gz
	SRR12513348_1.fastq.gz	Fastqsanger.gz

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Similar Datasets

Actin R256 mono-methylation is a conserved post-translational modification involved in transcription

Project description:Nuclear actin has been elusive due to the lack of molecular mechanisms. From actin-containing chromatin remodeling complexes, we discovered an arginine mono-methylation mark on evolutionarily conserved R256 residue of actin (R256me1). Actin R256 mutations in yeast affect nuclear functions, and cause diseases in human. Interestingly, we show that an antibody specific for actin R256me1 preferentially stain nuclear actin over cytoplasmic actin in yeast, mouse and human cells. We also show that actin R256me1 is regulated by protein arginine methyl transferase-5 (PRMT5) in HEK293 cells. Genome-wide survey of actin R256me1 mark provides a landscape for nuclear actin correlated with transcription. Further gene expression and protein interaction studies uncover extensive correlations between actin R256me1 and active transcription. The discovery of actin R256me1 mark suggests a fundamental mechanism to distinguish nuclear actin from cytoplasmic actin through post-translational modification (PTM), and potentially implicates an actin PTM mark in transcription and human diseases.

2020-08-26 | GSE156817 | GEO

Actin R256 Mono-methylation Is a Conserved Post-translational Modification Involved in Transcription.

Project description:Nuclear actin has been elusive due to the lack of knowledge about molecular mechanisms. From actin-containing chromatin remodeling complexes, we discovered an arginine mono-methylation mark on an evolutionarily conserved R256 residue of actin (R256me1). Actin R256 mutations in yeast affect nuclear functions and cause diseases in human. Interestingly, we show that an antibody specific for actin R256me1 preferentially stains nuclear actin over cytoplasmic actin in yeast, mouse, and human cells. We also show that actin R256me1 is regulated by protein arginine methyl transferase-5 (PRMT5) in HEK293 cells. A genome-wide survey of actin R256me1 mark provides a landscape for nuclear actin correlated with transcription. Further, gene expression and protein interaction studies uncover extensive correlations between actin R256me1 and active transcription. The discovery of actin R256me1 mark suggests a fundamental mechanism to distinguish nuclear actin from cytoplasmic actin through post-translational modification (PTM) and potentially implicates an actin PTM mark in transcription and human diseases.

| S-EPMC8860185 | biostudies-literature

Isoform-specific translational control is evolutionarily conserved in primates

Project description:Isoform-specific translational control is evolutionarily conserved in primates

| PRJNA961136 | ENA

Lysinoalanine crosslinking is a conserved post-translational modification in the spirochete flagellar hookLysinoalanine crosslinking is a conserved post-translational modification in the spirochete flagellar hook

Project description:In this project, we investigated whether diverse spirochete species contain lysinoalanine cross-linkages between conserved residues in their flagellar hook proteins (FlgE). We examined the following species: Treponema denticola¸ Borreliella burgdorferi, Treponema phagedenis, Treponema pallidum, Brachyspira hyodysenteriae, Leptospira interrogans. For each bacterial species, we examined a variety of different sample types, including recombinantly produced FlgE, polyhooks purified from flik knock-out strains, and wild-type periplasmic filaments. Overall, our data suggests that lysinoalanine crosslinking in a conserved FlgE post-translational modification in spirochetes and is required for the unique motility of these organisms. For more information, please see the following manuscript: https://doi.org/10.1101/2023.06.13.544825.

2024-01-26 | PXD045997 | Pride

Post-translational modification and regulation of actin.

Project description:Many of the best-studied actin regulatory proteins use non-covalent means to modulate the properties of actin. Yet, actin is also susceptible to covalent modifications of its amino acids. Recent work is increasingly revealing that actin processing and its covalent modifications regulate important cellular events. In addition, numerous pathogens express enzymes that specifically use actin as a substrate to regulate their hosts' cells. Actin post-translational alterations have been linked to different normal and disease processes and the effects associated with metabolic and environmental stressors. Herein, we highlight specific co-translational and post-translational modifications of actin and discuss the current understanding of the role that these modifications play in regulating actin.

| S-EPMC3578039 | biostudies-literature

Ubiquitination of the actin polymerase VASP

Project description:Filopodia are dynamic, actin-rich structures that extend outward from the cell to explore and respond to cues in the local environment. The actin polymerase VASP is a component of the filopodial tip complex, where it regulates actin polymerization and filopodial dynamics. Previously, we showed that VASP transiently co-localizes with the brain-enriched E3 ubiquitin ligase TRIM9 at the tips of neuronal filopodia. TRIM9 was required for the reversible, non-degradative ubiquitination of VASP and this modification was associated with decreased filopodia number and stability. Furthermore, the axon guidance cue netrin promoted deubiquitination of VASP. We hypothesize mono or multi-monoubiquitination of VASP is a mechanism to negatively regulate actin dynamics by blocking VASP and actin interactions. To determine the lysine residues that are ubiquitinated in VASP, we immunoprecipitated exogenously expressed human VASP from HEK293 cells. The immunopurified protein was analyzed by mass spectrometry to identify post-translational modifications. We identified numerous lysine residues that are ubiquitinated in VASP, including a high prevalence at K240 and K286.

2024-01-17 | PXD041196 | Pride

Isoform-specific translational control is evolutionarily conserved in primates

Project description:Alternative splicing (AS) influences the expression of human genes in diverse ways. We previously used subcellular fraction-sequencing (Frac-Seq) to reveal an unexpected connection between alternative splicing and isoform-specific mRNA translation. Here we apply comparative transcriptomics to explore alternative splicing coupled translational control (AS-TC) across 13 million years of primate evolution. We used Frac-seq to identify polyribosome associated mRNA isoforms from human, chimpanzee and orangutan induced pluripotent stem cell lines. We discovered orthologous AS-TC events with either conserved or species-specific translation patterns. Exons sequences associated with similar sedimentation profiles between species show strong sequence conservation compared to orthologous exons with divergent sedimentation profiles, suggesting exonic cis-regulatory elements influence to translational control. To test this hypothesis we created luciferase reporters from orthologous exons with divergent sedimentation profiles differing by a single nucleotide. Remarkably, single nucleotide substitutions were sufficient to drive species-specific expression of luciferase reporters. Together these data establish that cis-acting elements regulate AS-TC across primate species.

2024-04-30 | GSE230441 | GEO

Actin binding proteins expression levels when modifying the actin sequence

Project description:Actin binding proteins expression levels when modifying the actin sequence

| PRJNA782536 | ENA

Lso2 is a conserved ribosome-bound protein required for translational recovery in yeast

Project description:Lso2 is a conserved ribosome-bound protein required for translational recovery in yeast

| PRJNA430526 | ENA

RNA-seq data for: A conserved mito-cytoplasmic translational balance links two longevity pathways

Project description:Slowing down mRNA translation in either the cytoplasm or the mitochondria are both conserved longevity mechanisms. Here, we found a non-interventional natural correlation of mitochondrial and cytoplasmic ribosomal proteins when looking at mouse population genetics, suggesting a mito-cytoplasmic translational balance. Additionally, inhibiting mitochondrial translation in C. elegans in turn reduced cytoplasmic translation and repressed growth pathways while upregulating stress responses at both proteome and transcriptome levels. This coordinated repression of cytoplasmic translation is dependent on the atf-5/Atf4 transcription factor and is conserved in mammalian cells upon inhibiting mitochondrial translation pharmacologically with the antibiotic doxycycline. Lastly, extending this to a mammalian setting using doxycycline-treated germ-free mice, we found repressed cytoplasmic translation and ribosomal proteins in liver. These data demonstrate that inhibiting mitochondrial translation initiates a signaling cascade leading to coordinated repression of cytoplasmic translation, unlike previously described unidirectional cyto-to-mito translational communication in yeast, which can be targeted to promote healthy aging.

2019-12-11 | GSE122097 | GEO

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