ArticleMolecular and cellular biology2013
Casein kinase 2 associates with the yeast chromatin reassembly factor Spt2/Sin1 to regulate its function in the repression of spurious transcription.
Article in Molecular and cellular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 15 citations in OpenAlex.
- Direct prediction of intrinsically disordered protein conformational properties from sequence.Nature methods · 2024Article
- The histone chaperone SPT2 regulates chromatin structure and function in Metazoa.Nature structural & molecular biology · 2024Article
- Insights into Spt6: a histone chaperone that functions in transcription, DNA replication, and genome stability.Trends in genetics : TIG · 2023Review
- The catalytic subunit of Plasmodium falciparum casein kinase 2 is essential for gametocytogenesis.Communications biology · 2021Article
- SCRaMbLE generates evolved yeasts with increased alkali tolerance.Microbial cell factories · 2019Article
- Casein Kinase II Phosphorylation of Spt6 Enforces Transcriptional Fidelity by Maintaining Spn1-Spt6 Interaction.Cell reports · 2018Article
- Casein kinase 2 mediated phosphorylation of Spt6 modulates histone dynamics and regulates spurious transcription.Nucleic acids research · 2018Article
- Functional Analysis of Hif1 Histone Chaperone inG3 (Bethesda, Md.) · 2018Article
- Structure-function studies of histone H3/H4 tetramer maintenance during transcription by chaperone Spt2.Genes & development · 2015Article
- Association of the SPT2 chromatin protein domain containing 1 gene rs17579600 polymorphism and serum lipid traits.International journal of clinical and experimental pathology · 2015Article
- Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Spt2/Sin1 is a DNA binding protein with HMG-like domains. It plays a role in chromatin modulations associated with transcription elongation in Saccharomyces cerevisiae. Spt2 maintains the nucleosome level in coding regions and is important for the inhibition of spurious transcription in yeast. In this work, we undertook a biochemical approach to identify Spt2-interacting partners. Interestingly, casein kinase 2 (CK2) interacts with Spt2 and phosphorylates it in vitro as well as in vivo on two small regions, region I (RI) (amino acids 226 to 230) and RII (amino acids 277 to 281), located in its essential C-terminal domain. Mutation of the phosphorylation sites in RI and RII to acidic residues, thereby mimicking CK2 phosphorylation, leads to the inhibition of Spt2 function in the repression of spurious transcription and to a loss of its recruitment to coding regions. Inversely, depleting cells of CK2 activity leads to an increased Spt2 association with genes. We further show that Spt2 physically interacts with the essential histone chaperone Spt6 and that this association is inhibited in vitro and in vivo by CK2-dependent phosphorylation. Taken together, our data suggest that CK2 regulates the function of Spt2 by modulating its interaction with chromatin and the histone chaperone Spt6.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.