Plant PRMTs Broaden the Scope of Arginine Methylation

Ahmad, Ayaz; Cao, Xiaofeng

doi:10.1016/j.jgg.2012.04.001

Cited by 44 publications

(46 citation statements)

References 122 publications

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“…arginine methylation | protein arginine methyltransferase | AtPRMT5 | pre-mRNA splicing | Prp19C/NTC P rotein arginine methyltransferase 5 (PRMT5), a highly conserved type II protein arginine methyltransferase, transfers methyl groups to arginine residues, generating monomethylarginine and symmetric ω-N G , N′ G -dimethylarginine (SDMA) (1)(2)(3). In mammals, PRMT5 methylates and interacts with diverse proteins, including histones and other proteins, and has long been implicated in the modulation of a variety of processes, such as transcriptional regulation, RNA metabolism (4), apoptosis (5), signal transduction (6), and germ cell development (7).…”

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confidence: 99%

Recruitment of the NineTeen Complex to the activated spliceosome requires AtPRMT5

Deng

Wang

et al. 2016

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

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Protein arginine methylation, catalyzed by protein arginine methyltransferases (PRMTs), is involved in a multitude of biological processes in eukaryotes. Symmetric arginine dimethylation mediated by PRMT5 modulates constitutive and alternative pre-mRNA splicing of diverse genes to regulate normal growth and development in multiple species; however, the underlying molecular mechanism remains largely unknown. A genetic screen for suppressors of an Arabidopsis symmetric arginine dimethyltransferase mutant, atprmt5, identified two gain-of-function alleles of pre-mRNA processing factor 8 gene (prp8-8 and prp8-9), the highly conserved core component of the U5 small nuclear ribonucleoprotein (snRNP) and the spliceosome. These two atprmt5 prp8 double mutants showed suppression of the developmental and splicing alterations of atprmt5 mutants. In atprmt5 mutants, the NineTeen complex failed to be assembled into the U5 snRNP to form an activated spliceosome; this phenotype was restored in the atprmt5 prp8-8 double mutants. We also found that loss of symmetric arginine dimethylation of Sm proteins prevents recruitment of the NineTeen complex and initiation of spliceosome activation. Together, our findings demonstrate that symmetric arginine dimethylation has important functions in spliceosome assembly and activation, and uncover a key molecular mechanism for arginine methylation in pre-mRNA splicing that impacts diverse developmental processes.arginine methylation | protein arginine methyltransferase | AtPRMT5 | pre-mRNA splicing | Prp19C/NTC P rotein arginine methyltransferase 5 (PRMT5), a highly conserved type II protein arginine methyltransferase, transfers methyl groups to arginine residues, generating monomethylarginine and symmetric ω-N G , N′ G -dimethylarginine (SDMA) (1-3). In mammals, PRMT5 methylates and interacts with diverse proteins, including histones and other proteins, and has long been implicated in the modulation of a variety of processes, such as transcriptional regulation, RNA metabolism (4), apoptosis (5), signal transduction (6), and germ cell development (7). Both loss-of-function and overexpression of PRMT5 are fatal in mammals (8). AtPRMT5, the Arabidopsis homolog of PRMT5, regulates multiple aspects of plant growth and development, such as flowering time, growth rate, leaf morphology, sensitivity to stress conditions, and circadian rhythm, by modulating transcription, constitutive and alternative precursor mRNA (pre-mRNA) splicing of diverse genes (9-13). AtPRMT5 also mediates the symmetric arginine dimethylation of uridine-rich small nuclear ribonucleoproteins (U snRNPs) AtSmD1, D3, and AtLSm4 proteins, thus linking arginine methylation and splicing (10,11,13). However, the exact mechanism remains elusive.Pre-mRNA splicing occurs in the nucleus, removing introns and ligating exons (14). In eukaryotes, most introns are spliced in a series of reactions catalyzed by the spliceosome, which consists of five subcomplexes of U snRNPs and several non-snRNP factors. Each U snRNP contains distinct splicing...

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confidence: 99%

Recruitment of the NineTeen Complex to the activated spliceosome requires AtPRMT5

Deng

Wang

et al. 2016

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

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“…AtPRMT3 is required for proper pre-rRNA processing and ribosome biogenesis, a role distinct from those of other, previously reported AtPRMTs (29). The null mutants of only AtPRMT3, but not AtPRMT1a/1b (52), AtPRMT4a/4b (53), AtPRMT10 (39, 54), or AtPRMT5 (55-59), display developmental phenotypes resembling those of ribosome biogenesis mutants (23,24,40,43).…”

Section: Discussionmentioning

confidence: 74%

“…PRMT family members have been implicated in many essential biological processes, including ribosome biogenesis at the level of ribosome assembly (29)(30)(31). Arginine methylation of the ribosomal proteins RPS3 and RPS10 in human cells, catalyzed by PRMT1 and PRMT5, respectively, facilitates their proper assembly into the ribosome small subunit (32,33).…”

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Arabidopsis protein arginine methyltransferase 3 is required for ribosome biogenesis by affecting precursor ribosomal RNA processing

Hang

Liu

Ahmad

et al. 2014

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

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Ribosome biogenesis is a fundamental and tightly regulated cellular process, including synthesis, processing, and assembly of rRNAs with ribosomal proteins. Protein arginine methyltransferases (PRMTs) have been implicated in many important biological processes, such as ribosome biogenesis. Two alternative precursor rRNA (prerRNA) processing pathways coexist in yeast and mammals; however, how PRMT affects ribosome biogenesis remains largely unknown. Here we show that Arabidopsis PRMT3 (AtPRMT3) is required for ribosome biogenesis by affecting pre-rRNA processing. Disruption of AtPRMT3 results in pleiotropic developmental defects, imbalanced polyribosome profiles, and aberrant pre-rRNA processing. We further identify an alternative pre-rRNA processing pathway in Arabidopsis and demonstrate that AtPRMT3 is required for the balance of these two pathways to promote normal growth and development. Our work uncovers a previously unidentified function of PRMT in posttranscriptional regulation of rRNA, revealing an extra layer of complexity in the regulation of ribosome biogenesis.arginine methylation | protein arginine methyltransferase | AtPRMT3 | ribosome biogenesis | rRNA processing T he fundamental, complicated, and highly cooperative process of ribosome biogenesis involves ribosomal DNA (rDNA) transcription, precursor rRNA (pre-rRNA) processing, and assembly with ribosomal proteins and related assembly factors (1, 2). As a multistep, error prone, and energy-consuming process, ribosome biogenesis is also highly regulated (3, 4). In eukaryotic cells, mutations in ribosomal proteins or ribosome assembly factors usually lead to aberrant pre-rRNA processing (5-7) and activation of the polyadenylation-mediated RNA quality control system (4, 8, 9), resulting in various genetic diseases in humans (10, 11).Work in budding yeast, Saccharomyces cerevisiae, has deciphered the mechanisms of ribosome biogenesis (1, 2, 12). After transcription by RNA polymerase I and site-specific modification by small nucleolar ribonucleoproteins, the nascent 35S rRNA, the common precursor of 18S, 5.8S, and 25S rRNAs, is quickly assembled with many assembly factors and ribosomal proteins into small subunit processome/90S preribosomal particles (13-15). Then it mainly undergoes the "U3-dependent cleavage occurs first" pathway, which first removes the 5′ external transcribed sequence (5′ ETS) of 35S rRNA, to generate the 32S rRNA (16, 17). Next, after cleavage at the A2 site of intergenic transcribed sequence 1 (ITS1) between 18S rRNA and 5.8S rRNA, the 90S preribosomal particle splits into two independent complexes of pre-40S and pre-60S ribosomal particles. Finally, ribosomal subunits are further matured and assembled into 80S ribosomes for translation in the cytoplasm (12). However, in contrast to budding yeast, pre-rRNA processing in Xenopus laevis oocytes, mouse cells, and human cells preferentially cleave in ITS1 before the complete removal of the 5′ ETS (18-21), which may represent a common pathway in metazoans.In plants, a pre-rRNA processi...

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“…S3 and S10). Similarly, histone Arg methylation is catalyzed by a small group of protein Arg methyltransferases, including PRMT5, PRMT10, and PRMT4 (Ahmad and Cao, 2012). The phylogenetic tree showed that members of these three subfamilies are also highly conserved and mostly single copy, except for two copies of PRMT4 (PRMT4A and PRMT4B) due to the lineagespecific expansion in Brassicaceae (Supplemental Fig.…”

Section: Increase In the Complexity Of The Jmjc-mediated Histone Demementioning

confidence: 98%

Expansion and Functional Divergence of Jumonji C-Containing Histone Demethylases: Significance of Duplications in Ancestral Angiosperms and Vertebrates

et al. 2015

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Plant PRMTs Broaden the Scope of Arginine Methylation

Cited by 44 publications

References 122 publications

Recruitment of the NineTeen Complex to the activated spliceosome requires AtPRMT5

Recruitment of the NineTeen Complex to the activated spliceosome requires AtPRMT5

Arabidopsis protein arginine methyltransferase 3 is required for ribosome biogenesis by affecting precursor ribosomal RNA processing

Expansion and Functional Divergence of Jumonji C-Containing Histone Demethylases: Significance of Duplications in Ancestral Angiosperms and Vertebrates

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