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PRMT4 is a novel coactivator of c-Myb-dependent transcription in haematopoietic cell lines.

ABSTRACT: Protein arginine methyltransferase 4 (PRMT4)-dependent methylation of arginine residues in histones and other chromatin-associated proteins plays an important role in the regulation of gene expression. However, the exact mechanism of how PRMT4 activates transcription remains elusive. Here, we identify the chromatin remodeller Mi2? as a novel interaction partner of PRMT4. PRMT4 binds Mi2? and its close relative Mi2?, but not the other components of the repressive Mi2-containing NuRD complex. In the search for the biological role of this interaction, we find that PRMT4 and Mi2?/? interact with the transcription factor c-Myb and cooperatively coactivate c-Myb target gene expression in haematopoietic cell lines. This coactivation requires the methyltransferase and ATPase activity of PRMT4 and Mi2, respectively. Chromatin immunoprecipitation analysis shows that c-Myb target genes are direct transcriptional targets of PRMT4 and Mi2. Knockdown of PRMT4 or Mi2?/? in haematopoietic cells of the erythroid lineage results in diminished transcriptional induction of c-Myb target genes, attenuated cell growth and survival, and deregulated differentiation resembling the effects caused by c-Myb depletion. These findings reveal an important and so far unknown connection between PRMT4 and the chromatin remodeller Mi2 in c-Myb signalling.

SUBMITTER: Streubel G

PROVIDER: S-EPMC3591284 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature

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PRMT4 is a novel coactivator of c-Myb-dependent transcription in haematopoietic cell lines.

Streubel Gundula G Bouchard Caroline C Berberich Hannah H Zeller Marc S MS Teichmann Sophia S Adamkiewicz Jürgen J Müller Rolf R Klempnauer Karl-Heinz KH Bauer Uta-Maria UM

PLoS genetics 20130307 3

Protein arginine methyltransferase 4 (PRMT4)-dependent methylation of arginine residues in histones and other chromatin-associated proteins plays an important role in the regulation of gene expression. However, the exact mechanism of how PRMT4 activates transcription remains elusive. Here, we identify the chromatin remodeller Mi2α as a novel interaction partner of PRMT4. PRMT4 binds Mi2α and its close relative Mi2β, but not the other components of the repressive Mi2-containing NuRD complex. In t ...[more]

PMID: 23505388

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Project description:Tartary buckwheat (Fagopyrum tataricum Gaertn.) is a coarse cereal with strongly abiotic resistance. The MYB family plays a regulatory role in plant growth, development, and responses to biotic and abiotic stresses. However, the characteristics and regulatory mechanisms of MYB transcription factors in Tartary buckwheat remain unclarified. Here, this study cloned the FtMYB22 gene from Tartary buckwheat, and investigated its involvement in responding to individual water deficit and salt stress in Arabidopsis. Sequence analysis highlighted that the N-termini of FtMYB22 contained two highly conserved SANT domains and one conserved domain from the SG20 subfamily. Nucleus-localized FtMYB22 did not have individual transcriptional activation activity. Water deficiency and salt stress induced the high expression of the GUS gene, which was driven by the promoter of FtMYB22. Yeast stress experiments showed that the overexpression of FtMYB22 significantly reduced the growth activity of transgenic yeast under water deficit or salt stress. Consistently, the overexpression of FtMYB22 reduced the salt and water deficit stress resistance of the transgenic plants. In addition, physiological parameters showed that transgenic plants had lower proline and antioxidant enzyme activity under stress conditions. Compared to the wild-type (WT), transgenic plants accumulated more malondialdehyde (MDA), H2O2, and O2−; they also showed higher ion permeability and water loss rates of detached leaves under stress treatments. Notably, FtMYB22 was involved in plant stress resistance through an ABA-dependent pathway. Under stress conditions, the expression of RD29A, RD29B, PP2CA, KIN1, COR15A, and other genes in response to plant stress in transgenic lines was significantly lower than that in the WT (p < 0.05). Furthermore, yeast two-hybrid assay showed that there was a significant interaction between FtMYB22 and the ABA receptor protein RCAR1/2, which functioned in the ABA signal pathway. Altogether, FtMYB22, as a negative regulator, inhibited a variety of physiological and biochemical reactions, affected gene expression and stomatal closure in transgenic plants through the ABA-dependent pathway, and reduced the tolerance of transgenic Arabidopsis to water deficiency and salt stress. Based on these fundamental verifications, further studies would shed light on the hormone signal response mechanism of FtMYB22.

Dataset Information

PRMT4 is a novel coactivator of c-Myb-dependent transcription in haematopoietic cell lines.

Publications

PRMT4 is a novel coactivator of c-Myb-dependent transcription in haematopoietic cell lines.

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