RNA polymerase II-mediated transcription at active loci does not require histone H3S10 phosphorylation in<i>Drosophila</i>

Cai, Weili; Bao, Xiaomin; Huai, Dongxin; Jin, Ye; Girton, Jack; Johansen, Jørgen

doi:10.1242/dev.024927

Cited by 39 publications

(68 citation statements)

References 36 publications

(79 reference statements)

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“…JIL-1 mediates histone H3 phosphorylation at Serine 10 and maintains open chromatin structure in transcriptionally active regions of the genome (Wang et al 2001). However, despite its localization on active genes, definition of a direct role in transcription remains elusive (Ivaldi et al 2007;Cai et al 2008;Regnard et al 2011).…”

Section: Dosage Compensation In Drosophilamentioning

confidence: 99%

Dosage Compensation inDrosophila

Lucchesi

Kuroda

2015

Cold Spring Harb Perspect Biol

185

173

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SUMMARYDosage compensation in Drosophila increases the transcription of genes on the single X chromosome in males to equal that of both X chromosomes in females. Site-specific histone acetylation by the malespecific lethal (MSL) complex is thought to play a fundamental role in the increased transcriptional output of the male X. Nucleation and sequence-independent spreading of the complex to active genes serves as a model for understanding the targeting and function of epigenetic chromatin-modifying complexes. Interestingly, two noncoding RNAs are key for MSL assembly and spreading to active genes along the length of the X chromosome.

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Section: Dosage Compensation In Drosophilamentioning

confidence: 99%

Dosage Compensation inDrosophila

Lucchesi

Kuroda

2015

Cold Spring Harb Perspect Biol

185

173

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“…36,37 However, these results have been recently challenged and H3S10ph has been suggested, instead, to cause structural alterations of chromatin, counteracting heterochromatization and gene silencing at certain loci. 38 Indeed, in metazoa, as appears to be the case in Saccharomyces cerevisiae, 39 histone H3S10 phosphorylation may not be universally required for transcription but may play a distinct role tailored to specific promoters. 10,34,35,38 Intriguingly, H3S10ph, as part of a double of covalent histone modifications may not be universal.…”

Section: Histone H3 Phosphorylation During Interphasementioning

confidence: 99%

Histone H3 phosphorylation: Universal code or lineage specific dialects?

Cerutti¹,

Casas-Mollano²

2009

Epigenetics

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Post-translational modifications of histones modulate the functional landscape of chromatin and impinge on many DNA-mediated processes. Phosphorylation of histone H3 plays a role in the regulation of gene expression and in chromosome condensation/ segregation. Certain evolutionarily conserved residues on histone H3, namely Thr3, Ser10, Thr11 and Ser28, are phosphorylated during interphase or mitosis in both metazoa and plants. However, many of the kinases involved in these events appear to have evolved independently in different lineages. Likewise, the mechanistic function of specific phosphorylated amino acids, although poorly understood, also seems to differ among eukaryotes. Moreover, some modifications, such as phosphorylation of histone H3 Ser10, appear to have both a positive and a negative connotation and only become meaningful in combination with other histone marks within a particular chromatin context. Thus, a detailed understanding of the influence of histone H3 phosphorylation on biological processes may require learning organismal dialects of the histone code.

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“…Additional pathways for H3S10ph-mediated activation have been proposed, including a role in maintaining the active state of a gene, in part by preventing the spreading of H3K9me2 and HP1 and thus counteracting heterochromatin formation. [81][82][83] Thus, while the molecular events regulated by the dephosphorylation of H3S10 mediated by PP1 are currently unclear, our data suggest that phosphatase activities recruited by Sp3 play an important role in limiting the transition of RNA Pol II into productive elongation.…”

Section: Acknowledgmentsmentioning

confidence: 79%

Enforcing the pause: Transcription factor Sp3 limits productive elongation by RNA polymerase II

Valín

Gill²

2013

Cell Cycle

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Abbreviations: CDK, cyclin-dependent kinase; CTD, C-terminal domain of the RNA polymerase II; DSIF, DRB sensitivity-inducing factor; H3K4me3, histone H3 trimethylated at lysine 4; H3K36me3, histone H3 trimethylated at lysine 36; H3S10, histone H3 serine 10; NELF, negative elongation factor complex; P-TEFb, positive transcription elongation factor b; PP, protein phosphatase; p21 CIP1 , cyclin-dependent kinase inhibitor 1A; RNA Pol II, RNA polymerase II; SUMO, small ubiquitin-related modifier T he transition of paused RNA polymerase II into productive elongation is a highly dynamic process that serves to fine-tune gene expression in response to changing cellular environments. We have recently reported that the transcription factor Sp3 inhibits the transition of paused RNA Pol II to productive elongation at the promoter of the cyclin-dependent kinase inhibitor p21 CIP1 and other Sp3-repressed genes. Our studies support the view that Sp3 has three modes of action: activation, SUMO-Sp3-mediated heterochromatin silencing and SUMOindependent inhibition of elongation. At the p21 CIP1 promoter, binding of the positive elongation factor P-TEFb kinase was not affected by Sp3. In contrast, Sp3 promoted binding of the protein phosphatase PP1 to the p21 CIP1 promoter, suggesting that Sp3-dependent regulation of the local balance between kinase and phosphatase activities may contribute to gene expression. Our findings show that the transition of paused RNA Pol II to productive elongation is an important step regulated by both promoter-specific activators and repressors to finely modulate mRNA expression levels.

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RNA polymerase II-mediated transcription at active loci does not require histone H3S10 phosphorylation inDrosophila

Cited by 39 publications

References 36 publications

Dosage Compensation inDrosophila

Dosage Compensation inDrosophila

Histone H3 phosphorylation: Universal code or lineage specific dialects?

Enforcing the pause: Transcription factor Sp3 limits productive elongation by RNA polymerase II

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