Homo sapiens
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA107461 | ENA |
REPOSITORIES: ENA
Similar Datasets
Project description:Search for genes differently expressed when we inhibit NatB N-terminal acetyltransferase. We compare gene expression after inhibiting hNAT5 expression in Hela cells with specific siRNAs expressed with adenoviruses. Keywords: gene expression comparison
2008-03-12 | GSE10779 | GEO
Project description:Search for genes differently expressed when we inhibit NatB N-terminal acetyltransferase. We compare gene expression after inhibiting hNAT5 expression in Hela cells with specific siRNAs expressed with adenoviruses. Experiment Overall Design: We analyzed duplicate samples and we used as controls Hela cells and Hela cells that express a siRNA that doesn't inhibit any gene expression. Experiment Overall Design: The N-terminal acetyltransferase NatB, composed in Saccharomyces cerevisiae by the Nat3p and Mdm20p subunits, is an important factor for yeast growth and resistance to several stress agents. However, the expression and functional role of the mammalian counterpart has not yet been analysed. Here, we report the identification of Nat3p human homologue (hNAT5/hNAT3) and the characterization of its biological function. We found that hNAT5/hNAT3 silencing in HeLa cells results in inhibition of cell proliferation and increased sensitivity to the proapoptotic agent MG132. Moreover, inhibition of hNAT5/hNAT3 expression induces p53 activation and upregulation of the antiproliferative protein p21(WAF1/CIP1). The changes of the cellular transcriptome after hNAT5/hNAT3 knockdown confirmed the involvement of this protein in cell growth and survival processes. Among the genes differentially expressed we observed upregulation of several p53-dependent antiproliferative and proapoptotic genes. In the c-myc transgenic mice which is a model of inducible hepatocarcinoma we found that hNAT5/hNAT3 was upregulated when the tumor was induced. In accordance with this observation we noticed increased hNAT5/hNAT3 protein level in neoplastic versus non-neoplastic tissue in a high proportion of patients with hepatocellular carcinoma. Consequently, our results suggest that the expression of the protein hNAT5/hNAT3 is required for cellular proliferation and tumor growth.
2008-04-05 | E-GEOD-10779 | biostudies-arrayexpress
Project description:N-terminal acetyltransferase B (NatB) acetylates around 20% of the eukaryotic proteome and is crucial for protein function and organismal development. However, the regulatory roles of NatB-mediated N-terminal acetylation (NTA) in proteome stability and autophagy regulation remain unclear in plants. Our hypothesis is that the knockdown of Naa20 might alter the protein degradation at the global scale.
2026-03-01 | PXD066676 | Pride
Project description:In Arabidopsis thaliana the evolutionary conserved N-terminal acetyltransferase (Nat) complexes NatA and NatB co-translationally acetylate 60% of the proteome. Both have recently been implicated in the regulation of plant stress responses. While NatA mediates drought tolerance, NatB is required for pathogen resistance and the adaptation to high salinity and high osmolarity. Salt and osmotic stress impair protein folding and result in the accumulation of misfolded proteins in the endoplasmic reticulum (ER). The ER-membrane resident E3 ubiquitin ligase DOA10 targets misfolded proteins for degradation during ER stress and is conserved among eukaryotes. In yeast, DOA10 recognizes conditional degradation signals (Ac/N-degrons) created by NatA and NatB. Assuming that this mechanism is preserved in plants, the lack of Ac/N-degrons required for efficient removal of misfolded proteins might explain the sensitivity of NatB mutants to protein harming conditions. In this study, we investigate the response of NatB mutants to dithiothreitol (DTT) and tunicamycin (TM) induced ER stress. We report that NatB mutants are hypersensitive to DTT but not TM, suggesting that the DTT hypersensitivity is caused by an over-reduction of the cytosol rather than an accumulation of unfolded proteins in the ER. In line with this hypothesis, the cytosol of NatB depleted plants is constitutively over-reduced and a global transcriptome analysis reveals that their reductive stress response is permanently activated. Moreover, we demonstrate that doa10 mutants are susceptible to neither DTT nor TM, ruling out a substantial role of DOA10 in ER-associated protein degradation (ERAD) in plants. Contrary to previous findings in yeast, our data indicates that N-terminal acetylation (NTA) does not inhibit ER targeting of a substantial amount of proteins in plants. In summary, we provide further evidence that NatB-mediated imprinting of the proteome is vital for the response to protein-harming stress and rule out DOA10 as the sole recognin for substrates in the plant ERAD pathway.
2021-11-29 | GSE186324 | GEO
Project description: Not available
| S-EPMC2531291 | biostudies-literature
Project description:RNA extracted at 240min. Samples are rRNA depleted. Expression measurement of Homo sapiens genes.
2019-07-31 | GSE114179 | GEO
Project description:Alpha-synuclein (αSyn) protein levels correlate with the risk and severity of Parkinson's disease and related neurodegenerative diseases. Lowering αSyn is being actively investigated as a therapeutic modality. Here we systematically map the regulatory network that controls endogenous αSyn using sequential CRISPR-knockout and -interference screens in αSyn gene(SNCA) tagged cell lines and induced pluripotent stem cell-derived neurons (iNeurons). We uncover αSyn modifiers at multiple regulatory layers, with N-terminal acetyltransferase B (NatB) enzymes being the most potent endogenous αSyn modifier in both cell lines. N-terminal acetylation protects the cytosolic αSyn from rapid degradation by the proteasome in a Ube2Wdependent manner. Moreover, we show that pharmacological inhibition of methionylaminopeptidase 2 (METAP2), a regulator of NatB complex formation, attenuates endogenous αSyn in iNeurons carrying SNCA triplication. Together, our study reveals several gene networks that control endogenous αSyn, identifies mechanisms mediating the degradation of nonacetylated αSyn and illustrates potential therapeutic pathways for decreasing αSyn levels in synucleinopathies.
2024-05-22 | PXD048283 | Pride
Project description: Not available
| S-EPMC4686780 | biostudies-literature
Project description: Not available
| S-EPMC3743458 | biostudies-literature
Project description: Not available
| S-EPMC5738339 | biostudies-literature