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Acetylation - Europe PMC

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Last Updated: 10 November 2022

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Evaluating Histone Acetylation in Mouse Hematopoietic Stem and Progenitor Cells Using Chromatin Immunoprecipitation.

Epigenetics is the study of gene expression that does not change the DNA sequence. Epigenetic processes are natural and essential to cell functions; however, adverse effects can occur if they occur incorrectly or at the wrong time. Chromatin-DNA complexes can be modified by acetylation, altering chromatin structure, altering gene expression to influence gene expression. We have used Chromatin immunoprecipitation in HSPCs to learn epigenetic control in reaction to ionizing radiation.

Source link: https://europepmc.org/article/MED/36255693


Single-Cell Analysis of Histone Acetylation Dynamics at Replication Forks Using PLA and SIRF.

Genome integrity is continuously challenged by various methods, including DNA destruction, computerized DNA, transcription, and DNA-protein crosslinks. Accurate DNA replication is needed by DNA repair proteins, and forks must be able to combat these dangers. By acetylating histone H4 at lysine 8, the histone acetyltransferase PCAF, for example, has pushed forks to a deadlock forks. Here we have developed a comprehensive protocol that uses SIRF to detect the HAT PCAF and histone acetylation at replication forks.

Source link: https://europepmc.org/article/MED/36255636


Human Platelet Lysate as Valid Cell Growth Additive to Assess Protein Acetylation.

Cell cultures culture experiments are a viable alternative to animal experiments. We reported that lysine acetylation was very similar in cells in growth media containing FCS or human platelet lysate. In experiments with mammalian cell cultures, we discuss in detail how to produce and use hPL as a cost-effective substitute for FCS.

Source link: https://europepmc.org/article/MED/36255619


Drosophila CG17003/leaky (lky) is required for microtubule acetylation in early germ cells in Drosophila ovary.

By a gene of stable, long-lived microtubule acetylation is present in populations of stable, long-lived microtubules, based on the hydrated lysine 40 residue of u03b1-tubulin by acetyltransferases. In somatic follicle cells, we found that the absence of lky resulted in a progressive egg chamber fusion phenotype, as well as mislocalization of germline-specific Vasa protein. The observed mislocalization is likely caused by direct leakage of cellular fluids between germline and follicle cells, owing to chemical degradation of microtubules caused by Colcemid treatment's chemical disruption of microtubules, resulting in a mislocalization of Vasa in follicle cells in a short period of time.

Source link: https://europepmc.org/article/MED/36342916


Tropomyosin Cdc8 acetylation enhances binding to expressed S. pombe actin but does not promote differential association with fission yeast formins

According to the presence or absence of an amino-terminal acetylation that specifically identifies which formin-mediated F-actin networks it binds, it was suggested by cell research that S. pombe tropomyosin Cdc8 segregates into two groups. For investigation in vitro multicomponent mechanisms involving S. pombe actin, acetylated and unacetylated Tpm, formins Cdc12 and For3, as well as Myosins Myo2 and Myo51, we used 3-color TIRF microscopy to investigate in vitro multicomponent mechanisms involving S. pombe actin, acetylated and unacetylated Tpm, formins Despite a 12% sequence divergence between skeletal and S. pombe actin, S. pombe myosins Myo2 and Myo51 showed similar motile behaviour with the two actins, consistent with the structural finding that myosin interacts with a conserved footprint on actin. Although our vitro results support a direct formin-tropomyosin interaction, there is also the likelihood that formins bias differential tropomyosin isoform recruitment by unidentified mechanism involving additional proteins.

Source link: https://europepmc.org/article/PPR/PPR567123


Lin28A Reduced Sevoflurane-Induced Nerve Injury and Cognitive Dysfunction by Inhibiting Tau Acetylation and Phosphorylation via Activating SIRT1 in Elderly Rats.

Sevoflurane can cause neurotoxicity in elderly rats. Elderly rats were used to create an Sev-induced nerve injury model in this study. This research showed that Sev therapy caused nerve injury and cognitive impairment in elderly rats, as demonstrated by increased neuronal apoptosis and reduced Lin28A levels. Lin28A overexpression strongly halted Sev-induced neuronal apoptosis, according to TUNEL's report, and Lin28A overexpression significantly reversed Sev-induced neuronal apoptosis. Lin28A also boosted SIRT1 expression, which also reduced Sev-induced Tau acetylation in elderly rats' neurotylation and cognitive impairment in elderly rats, according to a new mechanistic review. In the enforcement of Lin28A in elderly rats, the introduction of SIRT1 inhibitor EX527 has also highlighted SIRT1's involvement in the regulation of Lin28A. Lin28A reduced sevoflurane-induced nerve injury and cognitive impairment by inhibiting Tau acetylation and phosphorylation in elderly rats by activating SIRT1.

Source link: https://europepmc.org/article/MED/36322362


Isoflurane impairs GluN2B-containing NMDA receptors trafficking and cognition via decreasing histone acetylation and EphB2 expression in aged hippocampal neurons.

Ioflurane exposure has been shown to cause cognitive decline, according to new medical research, but the exact molecular mechanisms remain unclear. We found that isoflurane reduced fear memory in aged mice, reduced GluN2B-containing NMDA receptor phosphorylation and trafficking, as well as the expression of EphB2, a key regulator of synaptic localization of NMDA receptors. We also found that isoflurane could raise the expression of HDAC2, which was also richer at the ephb2 gene promoter and tightly controlled transcription of ephb2.

Source link: https://europepmc.org/article/MED/36321664


A TDP-43 acetylation-mimic mutation that disrupts RNA-binding drives FTLD-like neurodegeneration in a mouse model of sporadic TDP-43 proteinopathy

Frontotemporal lobar dementia and amyotrophic lateral sclerosis are neurological disorders characterized by aggregation and mislocalization of TDP-43 proteinopathies, as well as subsequent neuronal disorders. Here, we produced an endogenous model of sporadic TDP-43 proteinopathy based on the principle that disease-associated TDP-43 acetylation at lysine 145 destabilizes TDP-43 conformation, reduces RNA-binding capacity, and causes downstream mis-regulation of target genes. TDP-43Q and lack-of-function in mouse primary neurons and human induced pluripotent stem cell-derived neurons were found in stress-induced phase-separated TDP-43 foci and loss-of-TDP-43-function in mouse primary neurons and human induced pluripotent stem cell-derived neurons.

Source link: https://europepmc.org/article/PPR/PPR565388


PARP-dependent acetylation of N4-cytidine in RNA appears in UV- damaged chromatin

In telophase, we find a notable positivity of ac4C RNA in DNA lesions of interphase cells and in irradiated cells. Our results show that acetylation of N4-cytidine in RNA is a key RNA modification that, with a high chance, aids DNA damage repair. Ac4C RNA likely contributes to de-condensation of chromatin in the vicinity of DNA lesions that are accessible to other DNA repair factors that play a role in DNA damage responses.

Source link: https://europepmc.org/article/PPR/PPR565369


Reduced acetylation of TFAM promotes bioenergetic dysfunction in the failing heart

Following transaortic constriction, we find that cardiomyocyte-specific GCN5L1 knockout mice in this study accelerated pressure overload-induced heart failure progression. Mitochondrial DNA and mitochondrial electron transport chain protein levels were reduced in cGCN5L1 KO hearts following TAC, and isolated neonatal cardiomyocytes with reduced GCN5L1 expression had lower bioenergetic output in response to hypertrophic strain. GCN5L1 expression loss caused to a decrease in the acetylation status of mitochondrial transcription factor A after TAC in vivo, which was traced to a decline in mtDNA levels in vitro.

Source link: https://europepmc.org/article/PPR/PPR565101

* Please keep in mind that all text is summarized by machine, we do not bear any responsibility, and you should always check original source before taking any actions

* Please keep in mind that all text is summarized by machine, we do not bear any responsibility, and you should always check original source before taking any actions