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How alteration in acetylation status might affect nuclear deformations and nuclear blebbing? 


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Alterations in acetylation status can impact nuclear deformations and blebbing by influencing nuclear architecture and stability. Acetylation, a crucial post-translational modification, regulates histone and non-histone proteins involved in various cellular processes, including nuclear integrity. Studies on cloned embryos show that histone acetylation levels in donor cells correlate with developmental potential, affecting cloning efficiency and nuclear stability. Additionally, induced differentiation in stem cells and cancer cells results in changes in histone acetylation patterns, indicating a role in cellular differentiation and nuclear structure. These findings suggest that acetylation alterations can lead to nuclear abnormalities, chromosomal instability, and impaired nuclear mechanostability, ultimately affecting nuclear deformations and blebbing.

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Changes in histone acetylation status during cell differentiation can influence nuclear deformations and blebbing by modulating chromatin structure and gene expression, impacting nuclear morphology.
Open accessJournal ArticleDOI
D Suhardjono, J Boutagy, GM Shenfield 
10 Citations
Not addressed in the paper.
Alteration in lamin A/C acetylation affects nuclear deformations by increasing solubility, impairing phosphorylation dynamics, and compromising nuclear mechanostability, leading to nuclear abnormalities and blebbing.
Alteration in acetylation status, such as treatment with NaBu, can impact histone acetylation levels and improve development of cloned embryos, potentially influencing nuclear deformations and blebbing during nuclear transfer.
Altered protein acetylation can impact nuclear deformations and blebbing by influencing the regulation of nuclear proteins involved in RNA metabolism and localization.

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What does acetylation do to replication forks?4 answersAcetylation of replication forks has various effects on DNA replication. Acetylation of the RRM2 subunit of ribonucleotide reductase (RNR) at K95 disrupts RNR activity and dNTP synthesis, leading to DNA replication fork stalling and reduced tumor cell growth. Acetylation of histone H3 by Rtt109 regulates fork velocity, with N-terminal acetylation slowing replication and K56 acetylation contributing to replication dynamics when N-terminal acetylation is compromised. Deacetylation of H2BK33 and trimethylation of H3K9 in nucleosomes surrounding stalling forks induce chromatin compaction, stabilizing the forks and preventing collapse. Acetylation of newly synthesized histone H4 by Hat1 during replication-coupled chromatin assembly is important for proper processing and assembly of newly synthesized histones, and loss of Hat1 leads to replication fork stalling and degradation of newly synthesized DNA.
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What are the consequences of loss of acetylation sites in androgen receptors?3 answersLoss of acetylation sites in androgen receptors has several consequences. Mutation of these sites affects the potency and efficacy of androgen-dependent response, particularly on certain promoters such as the Pem promoter. It also leads to delayed ligand-dependent nuclear translocation, misfolding, and aggregation of the receptor. Furthermore, loss of acetylation sites reduces trans-activation of androgen-responsive genes and impairs coactivation by various AR cofactors. The AR acetylation site mutants show reduced responsiveness to trichostatin A and ligand-induced phosphorylation. Additionally, loss of acetylation sites results in increased histone acetylation at AR and non-AR-regulated gene promoters, leading to enhanced AR activity and cell growth in response to all androgens, including weaker adrenal androgens. These findings suggest that acetylation of androgen receptors plays a crucial role in regulating their activity, subcellular distribution, and interaction with other proteins, ultimately influencing the transcriptional regulation of target genes.

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