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Investigation of the gamma-tubulin and PCNA binding site in the DNA of cells in S-phase

ABSTRACT: Investigation of the gamma-tubulin and PCNA binding site in the DNA of cells in S-phase

PROVIDER: PRJNA449960 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR7010980.fastq.gz	Fastqsanger.gz
	SRR7010981.fastq.gz	Fastqsanger.gz
	SRR7010974.fastq.gz	Fastqsanger.gz
	SRR7010975.fastq.gz	Fastqsanger.gz
	SRR7010976.fastq.gz	Fastqsanger.gz

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Investigation of the PCNA binding site in the DNA of cells in S-phase

2021-06-18 | GSE113094 | GEO

The g-tubulin meshwork assists to the transport of cytosolic PCNA to chromatin in mammalian cells

Project description:Changes in the location of g-tubulin ensure cell survival and preserve genome integrity. We investigated whether the nuclear accumulation of g-tubulin facilitates the transport of proliferating cell nuclear antigen (PCNA) between the cytosolic and the nuclear compartment in mammalian cells. We found that the g-tubulin meshwork assists to the recruitment of PCNA to chromatin. Also, decreased levels of g-tubulin reduce the nuclear pool of PCNA. In addition, the g-tubulin C terminus encodes a PCNA-interacting peptide (PIP) motif, and a g-tubulin–PIP-mutant affects the nuclear accumulation of PCNA. In a cell-free system, PCNA and g-tubulin formed a complex. In tumors, there is a significant positive correlation between TUBG1 and PCNA expression. Thus, we report a novel mechanism that constitutes the basis for tumor growth by which the g-tubulin meshwork maintains indefinite proliferation by acting as an opportune scaffold for the transport of PCNA from the cytosol to the chromatin.

2021-04-17 | GSE148798 | GEO

The g-tubulin meshwork assists to the transport of cytosolic PCNA to chromatin in mammalian cells

Project description:Changes in the location of g-tubulin ensure cell survival and preserve genome integrity. We investigated whether the nuclear accumulation of g-tubulin facilitates the transport of proliferating cell nuclear antigen (PCNA) between the cytosolic and the nuclear compartment in mammalian cells. We found that the g-tubulin meshwork assists to the recruitment of PCNA to chromatin. Also, decreased levels of g-tubulin affected the nuclear pool of PCNA. In addition, the g-tubulin C terminus encodes a PCNA-interacting peptide (PIP) motif, and a g-tubulin–PIP-mutant affects the nuclear accumulation of PCNA. In a cell-free system, PCNA and g-tubulin formed a complex. In tumors, there is a significant positive correlation between TUBG1 and PCNA expression. Thus, we report a novel mechanism that constitutes the basis for tumor growth by which the g-tubulin meshwork maintains indefinite proliferation by acting as an opportune scaffold for the transport of PCNA from the cytosol to the chromatin.

2021-06-18 | GSE173732 | GEO

Investigation of the gamma-tubulin binding site in the nuclear and mitochondrial DNA of cells in S-phase

Project description:In a cell, g-tubulin establishes a cellular network of threads named g-string meshwork. However, the functions of this meshwork remain to be determined. We investigated the traits of the meshwork and show that g-strings have the ability to connect the cytoplasm and the mitochondrial DNA together. We also show that g-tubulin has a role in the maintenance of the mitochondrial meshwork and homeostasis as reduced levels of g-tubulin or impairment of its GTPase domain disrupts the mitochondria network and alters both their respiratory capacity and the expression of mitochondria-related genes. By contrast, reduced mitochondria number or increased protein levels of g-tubulin DNA-binding domain favour the association of g-tubulin with mitochondria. Our results demonstrate that g-tubulin is an important mitochondrial structural component that maintains the mitochondria meshwork, providing mitochondria with a cellular infrastructure. We propose that g-tubulin provides a cytoskeletal element that maintains mitochondria homeostasis and gives form to the mitochondria meshwork. Keywords: Genome binding/occupancy profiling by high throughput sequencing

2018-04-04 | GSE107975 | GEO

Investigation of the gamma-tubulin binding site in the nuclear and mitochondrial DNA of cells in S-phase

Project description:Investigation of the gamma-tubulin binding site in the nuclear and mitochondrial DNA of cells in S-phase

| PRJNA422088 | ENA

Investigation of the PCNA binding site in the DNA of cells in S-phase

Project description:Investigation of the PCNA binding site in the DNA of cells in S-phase

| PRJNA449961 | ENA

The g-tubulin meshwork assists to the transport of cytosolic PCNA to chromatin in mammalian cells

Project description:The g-tubulin meshwork assists to the transport of cytosolic PCNA to chromatin in mammalian cells

| PRJNA625747 | ENA

The g-tubulin meshwork assists to the transport of cytosolic PCNA to chromatin in mammalian cells

Project description:The g-tubulin meshwork assists to the transport of cytosolic PCNA to chromatin in mammalian cells

| PRJNA726926 | ENA

RNA-seq of PCNA WT/PyMT mammary tumor cell and PCNA 211F mammary tumor cell

Project description:To further understand the cellular function of PCNA Y211 phosphrylation, we have profiled RNA expression from our transgenic mouse model derived mammary tumor cell.

2021-08-24 | GSE150513 | GEO

Structure of the native gamma-Tubulin Ring Complex capping spindle microtubules

Project description:Microtubules (MTs) are fundamental to cellular architecture, function and organismal development. They are nucleated from microtubule organizing centres by the evolutionary conserved ?-tubulin ring complex (?TuRC). However, the molecular mechanism of nucleation remains elusive. Here, we used cryo-electron tomography (cryo-ET) to determine the structure of the native ?TuRC capping the minus end of a MT in the context of enriched budding yeast spindles. In our structure, ?TuRC presents a ring of ?-tubulin subunits to seed nucleation of exclusively 13-protofilament microtubules, and it adopts an active closed conformation to function as a perfect geometric template for MT nucleation. Our cryo-ET reconstruction also revealed that a novel coiled-coil protein staples the first row of ?/?-tubulin molecules to alternating positions along the ?-tubulin ring. This positioning of ?/?-tubulin onto ?TuRC suggests a role for the coiled-coil protein in augmenting ?TuRC-mediated microtubule nucleation. Based on our results we describe a molecular model for budding yeast ?TuRC activation and MT nucleation.

2024-03-05 | PXD050372 | Pride

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