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Casein kinase II promotes piRNA production through direct phosphorylation of USTC component TOFU-4

ABSTRACT: Casein kinase II promotes piRNA production through direct phosphorylation of USTC component TOFU-4

PROVIDER: PRJNA998801 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR25431177.fastq.gz	Fastqsanger.gz
	SRR25431178.fastq.gz	Fastqsanger.gz
	SRR25431179.fastq.gz	Fastqsanger.gz
	SRR25431180.fastq.gz	Fastqsanger.gz
	SRR25431181.fastq.gz	Fastqsanger.gz

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Casein kinase II promotes piRNA production through direct phosphorylation of USTC component TOFU-4

Project description:Piwi-interacting RNAs (piRNAs) are genomically encoded small RNAs that engage Piwi Argonaute proteins to direct mRNA surveillance and transposon silencing. Despite advances in understanding piRNA pathways and functions, how the production of piRNA is regulated remains elusive. Here, using a genetic screen, we identify casein kinase II (CK2) as a factor required for piRNA pathway function. We show that CK2 is required for the localization of PRG-1 and for the proper localization of several factors that comprise the ‘upstream sequence transcription complex’ (USTC), which is required for piRNA transcription. Loss of CK2 impairs piRNA levels suggesting that CK2 promotes USTC function. We identify the USTC component twenty-one-U fouled-up 4 (TOFU-4) as a direct substrate for CK2. Our findings suggest that phosphorylation of TOFU-4 by CK2 promotes the assembly of USTC and piRNA transcription. Notably, during the aging process, CK2 activity declines, resulting in the disassembly of USTC, decreased piRNA production, and defects in piRNA-mediated gene silencing, including transposons silencing. These findings highlight the significance of posttranslational modification in regulating piRNA biogenesis and its implications for the aging process. Overall, our study provides compelling evidence for the involvement of a posttranslational modification mechanism in the regulation of piRNA biogenesis.

2024-07-01 | GSE239315 | GEO

Casein kinase II promotes piRNA production through direct phosphorylation of USTC component TOFU-4.

Project description:Piwi-interacting RNAs (piRNAs) are genomically encoded small RNAs that engage Piwi Argonaute proteins to direct mRNA surveillance and transposon silencing. Despite advances in understanding piRNA pathways and functions, how the production of piRNA is regulated remains elusive. Here, using a genetic screen, we identify casein kinase II (CK2) as a factor required for piRNA pathway function. We show that CK2 is required for the localization of PRG-1 and for the proper localization of several factors that comprise the 'upstream sequence transcription complex' (USTC), which is required for piRNA transcription. Loss of CK2 impairs piRNA levels suggesting that CK2 promotes USTC function. We identify the USTC component twenty-one-U fouled-up 4 (TOFU-4) as a direct substrate for CK2. Our findings suggest that phosphorylation of TOFU-4 by CK2 promotes the assembly of USTC and piRNA transcription. Notably, during the aging process, CK2 activity declines, resulting in the disassembly of USTC, decreased piRNA production, and defects in piRNA-mediated gene silencing, including transposons silencing. These findings highlight the significance of posttranslational modification in regulating piRNA biogenesis and its implications for the aging process. Overall, our study provides compelling evidence for the involvement of a posttranslational modification mechanism in the regulation of piRNA biogenesis.

| S-EPMC10978872 | biostudies-literature

Functional proteomics identified an upstream trancription complex promoting piRNA biogenesis

Project description:Here we used functional proteomics approaches to identify an upstream transcription complex (USTC) that is required for piRNA biogenesis. The complex contains PRDE-1, SNPC-4, TOFU-4, and TOFU-5, all of which are enriched on the two piRNA clusters on chromosome IV and form distinct piRNA foci in the nucleus.

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Functional proteomics identified a PICS complex required for piRNA maturation and chromosome segregation

Project description:Piwi-interacting RNAs (piRNAs) play significant roles in suppressing transposons and nonself nucleic acids, maintaining genome integrity, and defending against viral infections, and are essential for fertility in a variety of organisms. In C. elegans, most piRNA precursors are transcribed by RNA polymerase II in the nucleus and are subjected to a number of processing and maturation steps. However, the biogenesis of piRNAs is still not fully understood. We used functional proteomics to study piRNA biogenesis in C. elegans and identified a piRNA processing and chromosome segregation (PICS) complex. The PICS complex contains two known piRNA biogenesis factors, TOFU-6 and PID-1, and three new proteins PICS-1, TOST-1, and ERH-2, which exhibit dynamic localization among different subcellular compartments. In the germlines of gravid animals, the PICS complex contains TOFU-6/PICS-1/ERH-2/PID-1, is largely concentrated at the perinuclear granule zone and engages in piRNA processing. During early embryogenesis, the TOFU-6/PICS-1/ERH-2/TOST-1 complex accumulates in the nucleus and plays essential roles in chromosome segregation and cell division. Interestingly, the functions of these factors in mediating chromosome segregation are independent of piRNA production. Therefore, we speculate that differential compositions of PICS factors may help cells coordinate distinct cellular processes.

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Casein Kinase II Phosphorylation of Spt6 Enforces Transcriptional Fidelity by Maintaining Spn1-Spt6 Interaction

Project description:Spt6 is a histone chaperone that associates with RNA polymerase II and deposits nucleosomes in the wake of transcription. Although Spt6 has an essential function in nucleosome deposition, it is not known whether this function is regulated by post-translational modification. Here, we report that casein kinase II (CKII) phosphorylation of Spt6 directs nucleosome reassembly at the 5’ ends of a broad range of genes to prevent aberrant antisense transcription and enforce transcriptional directionality. Mechanistically, we show that interaction of Spt6 with Spn1 – a constitutive binding partner required for chromatin reassembly and full recruitment of Spt6 to genes is positively regulated by CKII phosphorylation of Spt6. Together, our study defines a previously unknown function for CKII phosphorylation in transcription, and further, highlights the importance of post-translational modification as a mechanism to fine-tune the functions of histone chaperones.

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Shutdown is a component of the Drosophila piRNA biogenesis machinery

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Monitoring Beta-casein phosphorylation and O-glycosylation over lactation reveals distinct differences between the proteome and endogenous peptidome

Project description:Human milk is a vital biofluid containing a myriad of molecular components to ensure an infants best start at a healthy life. One key component of human milk is Beta-casein, a protein which is not only a structural constituent of casein micelles but also a source of bioactive, often antimicrobial, peptides contributing to milks endogenous peptidome. Importantly, post-translational modifications (PTMs) like phosphorylation and glycosylation typically affect the function of proteins and peptides, but here our understanding of Beta-casein is critically limited. To uncover the scope of proteoforms and endogenous peptidoforms we utilized mass spectrometry (LC-MSMS) to achieve in-depth longitudinal profiling of Beta-casein from human milk, studying two donors across 16 weeks of lactation. We not only observed changes in Beta-caseins known protein and endogenous peptidome phosphorylation, but also in previously unexplored O-glycosylation. This newly discovered PTM of Beta-casein may be important as it resides on known Beta-casein-derived antimicrobial peptide sequences.

2021-05-20 | MSV000087464 | MassIVE

Casein Kinase II Phosphorylation of Spt6 Enforces Transcriptional Fidelity by Maintaining Spn1-Spt6 Interaction

Project description:Casein Kinase II Phosphorylation of Spt6 Enforces Transcriptional Fidelity by Maintaining Spn1-Spt6 Interaction

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Casein Kinase 2 Mediated Phosphorylation of Spt6 Modulates Histone dynamics and Regulates Spurious Transcription

Project description:Casein Kinase 2 Mediated Phosphorylation of Spt6 Modulates Histone dynamics and Regulates Spurious Transcription

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