Saccharomyces cerevisiae
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA143909 | ENA |
REPOSITORIES: ENA
Similar Datasets
Project description:Expression profiles of histone point mutants
| PRJNA172006 | ENA
Project description:Non-essential knockouts of KEOPS complex members and associated genes have been investigated by expression profiling.
2011-08-05 | E-TABM-1070 | biostudies-arrayexpress
Project description:Although the conserved type B histone acetyltransferase is known to regulate both cytoplasmic histone acetylation and nuclear nucleosome assembly, the coordination between the dual functions remains poorly understood. Our study revealed that the Arabidopsis thaliana type B histone acetyltransferase HAG2 interactions with the histone chaperones MSI2, MSI3, and NASP, as well as histones H3 and H4, resulting in the formation of a conserved NuB4 complex. Within this complex, HAG2, MSI2, and MSI3 constitute a histone acetylation module that acetylates newly synthesized histone H4 at lysine 5 and 12 sites in the cytoplasm. This module collaborates with NASP to maintain the abundance of H3 and H4 proteins in the cytoplasm, but it is not necessary for nucleosome assembly in the nucleus, which differs from the role of NuB4 complexes in other eukaryotes. Furthermore, we found that, within the nucleus, the collaborative actions of the histone acetylation module and NASP enhance chromatin accessibility near the transcription start sites of protein-coding genes, while showing a negative impact on chromatin accessibility near the transcription termination sites. This suggests that the Arabidopsis NuB4 complex is responsible for modulating chromatin accessibility across the entire genome, highlighting a plant-specific function of the NuB4 complex.
2024-10-25 | GSE259414 | GEO
Project description:Although the conserved type B histone acetyltransferase is known to regulate both cytoplasmic histone acetylation and nuclear nucleosome assembly, the coordination between the dual functions remains poorly understood. Our study revealed that the Arabidopsis thaliana type B histone acetyltransferase HAG2 interactions with the histone chaperones MSI2, MSI3, and NASP, as well as histones H3 and H4, resulting in the formation of a conserved NuB4 complex. Within this complex, HAG2, MSI2, and MSI3 constitute a histone acetylation module that acetylates newly synthesized histone H4 at lysine 5 and 12 sites in the cytoplasm. This module collaborates with NASP to maintain the abundance of H3 and H4 proteins in the cytoplasm, but it is not necessary for nucleosome assembly in the nucleus, which differs from the role of NuB4 complexes in other eukaryotes. Furthermore, we found that, within the nucleus, the collaborative actions of the histone acetylation module and NASP enhance chromatin accessibility near the transcription start sites of protein-coding genes, while showing a negative impact on chromatin accessibility near the transcription termination sites. This suggests that the Arabidopsis NuB4 complex is responsible for modulating chromatin accessibility across the entire genome, highlighting a plant-specific function of the NuB4 complex.
2024-10-25 | GSE259413 | GEO
Project description:Expression profiling of yeast kinase and phosphatase knockouts
| PRJNA133899 | ENA
Project description:Evidence suggests that the TAF1 subunit of TFIID is a histone acetyltransferase (HAT) that is functionally redundant with the Gcn5 HAT of the SAGA and ADA complexes. Here we test a number of predictions of this hypothesis by examining the in vivo histone acetylation targets of TAF1 and Gcn5, and re-examining the basis for the reported genome-wide functional redundancy between TAF1 and Gcn5. Our findings do not support a number of basic tenets of the hypothesis, thus bringing into question the physiological presence of any TAF1 HAT function in yeast. We have also conducted genome-wide expression profiles of numerous other HATs (Elp3, Hat1, Hpa2, Sas3) in an effort identify potential functional redundancy between TAF1 and other HATs, and find none. Further investigation of TAF1 and the Esa1 HAT re-affirm a link between histone H4 acetylation by Esa1, and TFIID binding via interactions with acetylated histone H4-binding protein Bdf1. Keywords: ChIP-chip, genetic modification
2006-03-20 | GSE3346 | GEO
Project description:Although the conserved type B histone acetyltransferase is known to regulate both cytoplasmic histone acetylation and nuclear nucleosome assembly, the coordination between the dual functions remains poorly understood. Our study revealed that the Arabidopsis thaliana type B histone acetyltransferase HAG2 interactions with the histone chaperones MSI2, MSI3, and NASP, as well as histones H3 and H4, resulting in the formation of a conserved NuB4 complex. Within this complex, HAG2, MSI2, and MSI3 constitute a histone acetylation module that acetylates newly synthesized histone H4 at lysine 5 and 12 sites in the cytoplasm. This module collaborates with NASP to maintain the abundance of H3 and H4 proteins in the cytoplasm, but it is not necessary for nucleosome assembly in the nucleus, which differs from the role of NuB4 complexes in other eukaryotes. Furthermore, we found that, within the nucleus, the collaborative actions of the histone acetylation module and NASP enhance chromatin accessibility near the transcription start sites of protein-coding genes, while showing a negative impact on chromatin accessibility near the transcription termination sites. This suggests that the Arabidopsis NuB4 complex is responsible for modulating chromatin accessibility across the entire genome, highlighting a plant-specific function of the NuB4 complex.
2024-10-25 | GSE259415 | GEO
Project description:Dynamic modification of histone proteins plays a key role in regulating gene expression. However, histones themselves can also be dynamic, which potentially affects the stability of histone modifications. To determine the molecular mechanisms of histone turnover we developed a parallel screening method for epigenetic regulators by analyzing chromatin states on DNA barcodes. Histone turnover was quantified by employing a genetic pulse-chase technique called RITE, which was combined with chromatin immunoprecipitation and high-throughput sequencing. In this screen, the NuB4/HAT-B complex, containing the conserved type B histone acetyltransferase Hat1, was found to promote histone turnover. Unexpectedly, the three members of this complex could be functionally separated from each other as well as from the known interacting factor and histone chaperone Asf1. Thus, systematic and direct interrogation of chromatin structure on DNA barcodes can lead to the discovery of genes and pathways involved in chromatin modification and dynamics.
2012-05-15 | GSE30168 | GEO
Project description:Evidence suggests that the TAF1 subunit of TFIID is a histone acetyltransferase (HAT) that is functionally redundant with the Gcn5 HAT of the SAGA and ADA complexes. Here we test a number of predictions of this hypothesis by examining the in vivo histone acetylation targets of TAF1 and Gcn5, and re-examining the basis for the reported genome-wide functional redundancy between TAF1 and Gcn5. Our findings do not support a number of basic tenets of the hypothesis, thus bringing into question the physiological presence of any TAF1 HAT function in yeast. We have also conducted genome-wide expression profiles of numerous other HATs (Elp3, Hat1, Hpa2, Sas3) in an effort identify potential functional redundancy between TAF1 and other HATs, and find none. Further investigation of TAF1 and the Esa1 HAT re-affirm a link between histone H4 acetylation by Esa1, and TFIID binding via interactions with acetylated histone H4-binding protein Bdf1. Keywords: genetic modification
2006-03-20 | GSE3345 | GEO