JPL SAF Metagenome
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA641034 | ENA |
REPOSITORIES: ENA
Similar Datasets
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Project description:The impact of depleting SAF-A (HNRNPU) on the genome-wide replication timing program in human hTERT-RPE1 cells was assessed by a single-cell replication timing analysis.
2021-12-15 | E-MTAB-10234 | biostudies-arrayexpress
Project description:RNA components seem to be required for the localization of SAF-A on chromatin. A SAF-A/RNA mesh model has been proposed and supported by super-resolved images, in which SAF-A forms a homogeneous mesh together with nuclear scaffolding RNA species to regulate chromatin structure. As an evolutionarily conserved RNA-binding protein, SAF-A has been reported to interact with a wide variety of RNAs in different cell types. Particularly, a recent study points out that repetitive non-coding sequences of pre-mRNAs and lncRNAs can serve as scaffold RNAs to counter chromatin compaction and maintain chromosome territory architecture together with SAF-A. At this moment, most studies have demonstrated the role of SAF-A/RNA in regulating interphase chromatin structure, and very few works have covered the role of SAF-A/RNA in mitosis. A recent study showed that SAF-A, together with most of its interacting RNAs, needs to be evicted from the condensing chromosomes during mitosis. This brings out an open question of how the SAF-A/RNA scaffold is disassembled and rebuilt when the cell enters and exits mitosis. Here, we showed that α-satellite RNA is dynamically expressed and stays associated with the centromeric chromatin throughout the mitotic cell cycle. Specific interactions between α-satellite RNA and SAF-A were observed both in vitro and in vivo. Depletion of either α-satellite RNA or SAF-A would lead to chromosome missegregation phenotypes during mitosis. More importantly, interfering with α-satellite RNA showed an evident effect on the chromatin relocalization of SAF-A, and further LAP2 upon mitosis exit. Therefore, we proposed that α-satellite RNA may act as a foundation stone for recruiting SAF-A scaffold upon mitosis exit.
2025-03-25 | GSE270307 | GEO
Project description:Analysis of gene expression by RNA-seq upon siRNA mediated knockdown of scaffold attachment factor A (SAF-A) versus control siRNA in RPE1 cells at 24 hour and 48 hour time points post transfection reveals SAF-A loss does not impact on gene transcription
2017-06-01 | GSE98541 | GEO
Project description:α-satellite RNA has been shown to interact with specific sets of RNA-binding proteins. By forming complexes with centromere proteins CENPA, CENPB, and CENPC, α-satellite RNA demonstrated its essential role in maintaining functional human centromeres. Also, α-satellite RNA has been reported to interact with SUV39H1, which is the histone methyltransferase that is responsible for H3K9me3. Together with the findings in mice and some other eukaryotes that RNA components are required for the recruitment of heterochromatin proteins and the maintenance of pericentric heterochromatin, it has long been suspected that α-satellite RNA might also be involved in the heterochromatin formation and recruitment of HP1 in human cells. In this study, we identified Scaffold Attachment Factor-A (SAF-A) as a novel α-satellite RNA binding protein. SAF-A, also known as hnRNPU, the most abundant member in the hnRNP complex, was initially identified as the major component of the nuclear scaffold. It binds to the nuclear scaffold in AT-rich regions through its DNA-binding domain. In recent years, several studies have suggested that SAF-A may play a more fundamental and general role in nuclear organization in interphase. Depletion of SAF-A will lead to pronounced chromatin condensation of gene-rich regions and global changes in 3D genome architecture.
2025-03-31 | GSE286152 | GEO
Project description:Oryza sativa Japonica Group SAF, F-box protein, Indica-Japonica hybrid male sterilit, is differentially expressed in 5 experiment(s);
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Project description:α-satellite RNA has been shown to interact with specific sets of RNA-binding proteins. By forming complexes with centromere proteins CENPA, CENPB, and CENPC, α-satellite RNA demonstrated its essential role in maintaining functional human centromeres. Also, α-satellite RNA has been reported to interact with SUV39H1, which is the histone methyltransferase that is responsible for H3K9me3. Together with the findings in mice and some other eukaryotes that RNA components are required for the recruitment of heterochromatin proteins and the maintenance of pericentric heterochromatin, it has long been suspected that α-satellite RNA might also be involved in the heterochromatin formation and recruitment of HP1 in human cells. In this study, we identified Scaffold Attachment Factor-A (SAF-A) as a novel α-satellite RNA binding protein. SAF-A, also known as hnRNPU, the most abundant member in the hnRNP complex, was initially identified as the major component of the nuclear scaffold. It binds to the nuclear scaffold in AT-rich regions through its DNA-binding domain. In recent years, several studies have suggested that SAF-A may play a more fundamental and general role in nuclear organization in interphase. Depletion of SAF-A will lead to pronounced chromatin condensation of gene-rich regions and global changes in 3D genome architecture.
2025-03-25 | GSE286151 | GEO
Project description:Drosophila melanogaster Saf-B, Scaffold attachment factor B, is differentially expressed in 10 experiment(s);
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