The arginine methyltransferase Rmt2 is enriched in the nucleus and co-purifies with the nuclear porins Nup49, Nup57 and Nup100

Olsson, Ida; Berrez, Jean-Marc; Leipus, Arunas; Östlund, Cecilia; Mutvei, Ann

doi:10.1016/j.yexcr.2007.03.007

Cited by 7 publications

(9 citation statements)

References 54 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…However, the association of Rmt2 with rpL12 and/or ribosomes, as well as the role of Rmt2 in ribosome function, remains elusive. The association between Rmt2 and specific nucleoporins was also recently demonstrated (68). Without any functional data, however, the role of Rmt2 in biological activities related to the ribosome and the nuclear pore complex remains to be established.…”

Section: Type IV Protein Arginine Methyltransferasesmentioning

confidence: 89%

“…Nevertheless, an unusual PRMT that catalyzes methylation of the delta (␦) nitrogen atom of arginines within proteins has been identified in S. cerevisiae (67,109). This arginine methyltransferase, designated Rmt2, is not essential for cell viability and accumulates in granulated and punctuated structures in both the nucleus and the cytoplasm of yeast cells, as determined by fluorescence microscopy (67,68). Interestingly, whereas the ability of budding yeast PRMT1 to modify protein substrates is not affected by translational inhibitors (101), Rmt2 appears to act on protein substrates in a cotranslational manner (67).…”

Section: Type IV Protein Arginine Methyltransferasesmentioning

confidence: 99%

See 1 more Smart Citation

Protein Arginine Methyltransferases: from Unicellular Eukaryotes to Humans

2007

View full text Add to dashboard Cite

Section: Type IV Protein Arginine Methyltransferasesmentioning

confidence: 89%

Section: Type IV Protein Arginine Methyltransferasesmentioning

confidence: 99%

Protein Arginine Methyltransferases: from Unicellular Eukaryotes to Humans

2007

View full text Add to dashboard Cite

“…Rmt2 is located in both in the nucleus and the cytoplasm of S. cerevisiae and copurifies with several nuclear pore components (87).…”

Section: An Unusual Protein Arginine Methyltransferase That Modifies mentioning

confidence: 99%

“…Importantly, a genome-wide transcription study of yeast cells deleted in the RMT2 gene revealed down regulation of a gene encoding the type II myosin heavy chain (87). In a high-throughput study, an Rmt2-green fluorescent protein fusion protein was shown to relocate to the nucleus after DNA damage in yeast cells induced by hydroxyurea or methyl methanesulfonate (88).…”

Section: An Unusual Protein Arginine Methyltransferase That Modifies mentioning

confidence: 99%

The ribosome: A hot spot for the identification of new types of protein methyltransferases

Clarke¹

2018

Journal of Biological Chemistry

View full text Add to dashboard Cite

Cellular physiology depends on the alteration of protein structures by covalent modification reactions. Using a combination of bioinformatic, genetic, biochemical, and mass spectrometric approaches, it has been possible to probe ribosomal proteins from the yeast Saccharomyces cerevisiae for posttranslationally methylated amino acid residues and for the enzymes that catalyze these modifications. These efforts have resulted in the identification and characterization of the first protein histidine methyltransferase, the first N-terminal protein methyltransferase, two unusual types of protein arginine methyltransferases, and a new type of cysteine methylation. Two of these enzymes may modify their substrates during ribosomal assembly because the final methylated histidine and arginine residues are buried deep within the ribosome with contacts only with RNA. Two of these modifications occur broadly in eukaryotes, including humans, while the others demonstrate a more limited phylogenetic range. Analysis of strains where the methyltransferase genes are deleted has given insight into the physiological roles of these modifications. These reactions described here add diversity to the modifications that generate the typical methylated lysine and arginine residues previously described in histones and other proteins. Regulation of biological function by protein methylation reactionsIt is more and more apparent just how much of biological function is dependent upon posttranslational modifications (1). The human genome encodes some 900 enzymes catalyzing just protein phosphorylation or ubiquitination (2,3). However, it is now clear that methyl groups can stand beside phosphate groups and ubiquitin as major players in controlling the physiological functions of proteins. We are beginning to understand how the much greater diversity of protein methylation reactions can give rise to a greater diversity of function (1,4-8). We are also learning the importance of crosstalk between protein and DNA methylation reactions (9) and among protein methylation, phosphorylation, acetylation, and ubiquitination reactions (10-12). Finally, we are discovering how alterations in protein methylation pathways can lead to human pathology, particularly in cancer (13-15).The collection of over sixty human protein arginine and lysine methyltransferases that leave histone "marks" recognized by reader proteins to guide gene expression are perhaps the poster children for the importance of protein methyltransferases (16-17). However, recent work has emphasized the importance of methylating non-histone substrates at these residues, particularly ribosomal proteins, translation factors, and transcription factors in a wide variety of organisms (7,8,15,18,19). Furthermore, the methylation of lysine and arginine residues represents just the tip of the iceberg in protein methylation -modifications have also been established at histidine, modified histidine (diphthamide), glutamate, glutamine, asparagine, Lisoaspartate, D-aspartate, cysteine, isoprenylcysteine, me...

show abstract

“…Fractionation of RibosomesFractionation of ribosomes from the wild-type and ⌬set11 mutant S. pombe strains was performed as described previously (34).…”

Section: Analysis Of Methylated Peptide By Nano-liquid Chromatographymentioning

confidence: 99%

A Conserved SET Domain Methyltransferase, Set11, Modifies Ribosomal Protein Rpl12 in Fission Yeast

Sadaie

Shinmyozu²,

Nakayama

2008

Journal of Biological Chemistry

View full text Add to dashboard Cite

SET domain-containing methyltransferases post-translationally modify a variety of cellular proteins, such as histones, cytochrome c, ribulose-bisphosphate carboxylase/oxygenase, and ribosomal proteins. In the fission yeast Schizosaccharomyces pombe, at least 13 SET domain-containing proteins have been identified in the genome, four of which are involved in transcriptional regulation through their modification of histone tails. However, the roles played by the other SET domain proteins in cellular processes and their physiological substrates remain unresolved. We show here that S. pombe Set11, a SET domaincontaining protein encoded by SPCC1223.04c, specifically modifies Rpl12 (ribosomal protein L12). Recombinant Set11 prepared from Escherichia coli had catalytic activity and methylated a 17-kDa polypeptide in cellular extracts of set11 mutant cells. The methylated protein was isolated by two-dimensional gel electrophoresis or by reverse-phase chromatography and was identified as Rpl12 by mass spectrometry. In vitro methylation experiments using wild-type and mutant Rpl12 proteins verified that Set11 modified recombinant Rpl12 and suggested that its potential target site was lysine 3. The methylation site modified by Set11 was also confirmed by mass spectrometric analysis, which also revealed other unique methylation sites of Rpl12. Finally, we found that Set11 predominantly localized to the nucleolus and that the overproduction of Set11 caused a severe growth defect. These results suggest that Rpl12 methylation occurs during the ribosomal assembly processes and that control of the Set11 expression level is important for its cellular function.

show abstract

The arginine methyltransferase Rmt2 is enriched in the nucleus and co-purifies with the nuclear porins Nup49, Nup57 and Nup100

Cited by 7 publications

References 54 publications

Protein Arginine Methyltransferases: from Unicellular Eukaryotes to Humans

Protein Arginine Methyltransferases: from Unicellular Eukaryotes to Humans

The ribosome: A hot spot for the identification of new types of protein methyltransferases

A Conserved SET Domain Methyltransferase, Set11, Modifies Ribosomal Protein Rpl12 in Fission Yeast

Contact Info

Product

Resources

About