SKB1-mediated symmetric dimethylation of histone H4R3 controls flowering time in Arabidopsis

Wang, Xin; Ya, Zhang; Ma, Qibin; Zhang, Zhaoliang; Xue, Yongbiao; Bao, Shilai; Chong, Kang

doi:10.1038/sj.emboj.7601647

Cited by 132 publications

(148 citation statements)

References 56 publications

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“…In this role, PRMT5 can be targeted to specific genes as well as exerting more ubiquitous effects. In Arabidopsis, PRMT5 has been shown to methylate R3 of histone H4 (H4R3sme2) at the Flowering locus C (FLC) promoter, which decreases expression of FLC, a flowering repressor, to promote flowering (27)(28)(29). Loss of PRMT5 function elevates FLC expression and therefore would lengthen period, which lengthens in response to increased FLC expression (39,48,49).…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Type II protein arginine methyltransferase 5 (PRMT5) is required for circadian period determination in Arabidopsis thaliana

Hong

Song

Lutz

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

118

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Posttranslational modification is an important element in circadian clock function from cyanobacteria through plants and mammals. For example, a number of key clock components are phosphorylated and thereby marked for subsequent ubiquitination and degradation. Through forward genetic analysis we demonstrate that protein arginine methyltransferase 5 (PRMT5; At4g31120) is a critical determinant of circadian period in Arabidopsis. PRMT5 is coregulated with a set of 1,253 genes that shows alterations in phase of expression in response to entrainment to thermocycles versus photocycles in constant temperature. PRMT5 encodes a type II protein arginine methyltransferase that catalyzes the symmetric dimethylation of arginine residues (Rsme2). Rsme2 modification has been observed in many taxa, and targets include histones, components of the transcription complex, and components of the spliceosome. Neither arginine methylation nor PRMT5 has been implicated previously in circadian clock function, but the period lengthening associated with mutational disruption of prmt5 indicates that Rsme2 is a decoration important for the Arabidopsis clock and possibly for clocks in general.circadian rhythms | circadian clock | luciferase

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Section: Discussionmentioning

confidence: 99%

“…We identified a mutant defective in Protein arginine methyltransferase 5 (PRMT5). Loss of PRMT5 activity confers late flowering (27)(28)(29). We show that prmt5 mutants exhibit lengthened periods in several circadian rhythms, including cotyledon movement and the expression of multiple clock genes and clock-controlled output genes.…”

mentioning

confidence: 99%

Type II protein arginine methyltransferase 5 (PRMT5) is required for circadian period determination in Arabidopsis thaliana

Hong

Song

Lutz

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

118

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“…SKB1 is a homolog of a human arginine methylase (PRMT5) that catalyses the symmetric dimethylation of H4R3 (H4R3sme2) and binds the FLC promoter; skb1 loss-of-function mutations result in upregulation of FLC and late flowering that can be reversed by vernalization. Furthermore skb1 mutants show decreased H4R3sme2 in regulatory regions of FLC, suggesting that this histone covalent modification is also required for the induction of flowering mediated by FLC repression (Pei et al, 2007;Wang et al, 2007;Schmitz et al, 2008).…”

Section: Flc Repression the Vernalised Statementioning

confidence: 99%

Chromatin remodeling in plant development

Jarillo¹,

Piñeiro²,

Cubas³

et al. 2009

Int. J. Dev. Biol.

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“…AtPRMT5 deficiency causes pleiotropic phenotypes, including delayed flowering, growth retardation, dark green and curled leaves, and reduced sensitivity to vernalization (22)(23)(24), implying a critical role for AtPRMT5 in regulating essential developmental processes in Arabidopsis. However, how AtPRMT5 impacts these biological processes is largely unknown.…”

mentioning

confidence: 99%

Arginine methylation mediated by the Arabidopsis homolog of PRMT5 is essential for proper pre-mRNA splicing

Deng

Gu²,

Liu³

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

169

182

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Protein arginine methylation, one of the most abundant and important posttranslational modifications, is involved in a multitude of biological processes in eukaryotes, such as transcriptional regulation and RNA processing. Symmetric arginine dimethylation is required for snRNP biogenesis and is assumed to be essential for pre-mRNA splicing; however, except for in vitro evidence, whether it affects splicing in vivo remains elusive. Mutation in an Arabidopsis symmetric arginine dimethyltransferase, AtPRMT5, causes pleiotropic developmental defects, including late flowering, but the underlying molecular mechanism is largely unknown. Here we show that AtPRMT5 methylates a wide spectrum of substrates, including some RNA binding or processing factors and U snRNP AtSmD1, D3, and AtLSm4 proteins, which are involved in RNA metabolism. RNA-seq analyses reveal that AtPRMT5 deficiency causes splicing defects in hundreds of genes involved in multiple biological processes. The splicing defects are identified in transcripts of several RNA processing factors involved in regulating flowering time. In particular, splicing defects at the flowering regulator FLOWERING LOCUS KH DOMAIN (FLK) in atprmt5 mutants reduce its functional transcript and protein levels, resulting in the up-regulation of a flowering repressor FLOWERING LOCUS C (FLC) and consequently late flowering. Taken together, our findings uncover an essential role for arginine methylation in proper premRNA splicing that impacts diverse developmental processes. P RMT5 is a type II protein arginine methyltransferase that catalyzes the formation of monomethylarginine and symmetric ω-N G , N′ G -dimethylarginine (SDMA) (1). PRMT5 is highly conserved among yeast, animals, and higher plants, and is implicated in diverse cellular and biological processes, including transcriptional regulation, RNA metabolism (1, 2), ribosome biogenesis (3), Golgi apparatus structure maintenance (4), and cell cycle regulation (5). In mouse, fly, and worm, PRMT5 orthologs are involved in germ-cell formation, specification, and maintenance (6-10).In mammalian cells, PRMT5 localizes to both the cytoplasm and the nucleus, and methylates multiple histone and nonhistone proteins (1). In the nucleus, PRMT5 usually functions in repressing target genes by methylating histone H4 Arginine 3 (H4R3), H3R8, as well as transcription factors/regulators (5, 11, 12). In the cytoplasm, PRMT5 mainly exists in a 20S methylosome complex, consisting of spliceosomal U snRNP (uridinerich small nuclear riboucleoprotein particles) Sm proteins (including Sm B/B′, D1, D2, D3, E, F, and G), PRMT5, pICln, and WD repeat protein/MEP50 (13-15). In this complex, U1, 2, 4, 5 snRNP Sm proteins Sm B/B′, D1, D3, and U6 snRNP-specific Sm-like protein LSm4 are symmetrically dimethylated by PRMT5 (13,16). Such methylation can increase the binding affinity of these Sm proteins for the downstream recipient, Survival Motor Neuron, the spinal muscular atrophy disease gene product (17,18). Subsequently, the PRMT5-and Survival Motor Neuroncom...

show abstract

SKB1-mediated symmetric dimethylation of histone H4R3 controls flowering time in Arabidopsis

Cited by 132 publications

References 56 publications

Type II protein arginine methyltransferase 5 (PRMT5) is required for circadian period determination in Arabidopsis thaliana

Type II protein arginine methyltransferase 5 (PRMT5) is required for circadian period determination in Arabidopsis thaliana

Chromatin remodeling in plant development

Arginine methylation mediated by the Arabidopsis homolog of PRMT5 is essential for proper pre-mRNA splicing

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