ArticleThe Journal of biological chemistry2016
Multifaceted Histone H3 Methylation and Phosphorylation Readout by the Plant Homeodomain Finger of Human Nuclear Antigen Sp100C.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 29 citations in OpenAlex.
- Sp140L functions as a herpesvirus restriction factor suppressing viral transcription and activating interferon-stimulated genes.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- SP140 represses specific loci by recruiting polycomb repressive complex 2 and NuRD complex.Nucleic acids research · 2025Article
- It Runs in the Bromodomain Family: Speckled Proteins (SP) Play a Role in the Antitumor Immune Response in Solid Tumors.International journal of molecular sciences · 2022Article
- PML Body Component Sp100A Is a Cytosolic Responder to IFN and Activator of Antiviral ISGs.mBio · 2022Article
- Immune chromatin reader SP140 regulates microbiota and risk for inflammatory bowel disease.Cell host & microbe · 2022Article
- PML Body Component Sp100A Restricts Wild-Type Herpes Simplex Virus 1 Infection.Journal of virology · 2022Article
- Functional Roles of Bromodomain Proteins in Cancer.Cancers · 2021Review
- Optimization of Alchemical Pathways Using Extended Thermodynamic Integration.Journal of chemical theory and computation · 2021Article
- The Speckled Protein (SP) Family: Immunity's Chromatin Readers.Trends in immunology · 2020Review
- Characterization of the plant homeodomain (PHD) reader family for their histone tail interactions.Epigenetics & chromatin · 2020Article
- The Fate of Speckled Protein 100 (Sp100) During Herpesviruses Infection.Frontiers in cellular and infection microbiology · 2020Review
- Integrative analysis reveals functional and regulatory roles of H3K79me2 in mediating alternative splicing.Genome medicine · 2018Article
- A systems medicine approach reveals disordered immune system and lipid metabolism in multiple sclerosis patients.Clinical and experimental immunology · 2018Article
- Sp100 colocalizes with HPV replication foci and restricts the productive stage of the infectious cycle.PLoS pathogens · 2017Article
- Understanding the Phosphorylation Mechanism by Using Quantum Chemical Calculations and Molecular Dynamics Simulations.The journal of physical chemistry. B · 2017Article
- Maintenance of macrophage transcriptional programs and intestinal homeostasis by epigenetic reader SP140.Science immunology · 2017Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The decoding of histone post-translational modifications by chromatin-binding modules ("readers") constitutes one major mechanism of epigenetic regulation. Nuclear antigen Sp100 (SPECKLED, 100 kDa), a constitutive component of the promyelocytic leukemia nuclear bodies, plays key roles in intrinsic immunity and transcriptional repression. Sp100C, a splicing isoform specifically up-regulated upon interferon stimulation, harbors a unique tandem plant homeodomain (PHD) finger and bromodomain at its C terminus. Combining structural, quantitative binding, and cellular co-localization studies, we characterized Sp100C PHD finger as an unmethylated histone H3 Lys(4) (H3K4me0) reader that tolerates histone H3 Thr(3) phosphorylation (H3T3ph), histone H3 Lys(9) trimethylation (H3K9me3), and histone H3 Ser(10) phosphorylation (H3S10ph), hallmarks associated with the mitotic chromosome. In contrast, whereas H3K4me0 reader activity is conserved in Sp140, an Sp100C paralog, the multivalent tolerance of H3T3ph, H3K9me3, and H3S10ph was lost for Sp140. The complex structure determined at 2.1 Å revealed a highly coordinated lysine ϵ-amine recognition sphere formed by an extended N-terminal motif for H3K4me0 readout. Interestingly, reader pocket rigidification by disulfide bond formation enhanced H3K4me0 binding by Sp100C. An additional complex structure solved at 2.7 Å revealed that H3T3ph is recognized by the arginine residue, Arg(713), that is unique to the PHD finger of Sp100C. Consistent with a restrictive cellular role of Sp100C, these results establish a direct chromatin targeting function of Sp100C that may regulate transcriptional gene silencing and promyelocytic leukemia nuclear body-mediated intrinsic immunity in response to interferon stimulation.
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