Identification of arginine- and lysine-methylation in the proteome of Saccharomyces cerevisiae and its functional implications

Pang, Chi Nam Ignatius; Gasteiger, Elisabeth; Wilkins, Marc R.

doi:10.1186/1471-2164-11-92

Cited by 84 publications

(100 citation statements)

References 82 publications

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“…MK motif appears to be evolutionarily conserved through eukaryotic cells, and Pang et al also noticed the same motif for methylated lysine from a much smaller protein data set in Saccharomyces cerevisiae. 28 Lysine and arginine methyltransferases seem to have distinct protein target specificities. In contrast to arginine methylation, we Normal (normal medium-cultured sample) and heavy ( 13 CD 3 -methionine medium-cultured sample), respectively.…”

Section: Resultsmentioning

confidence: 99%

Large-scale global identification of protein lysine methylation in vivo

Arnaudo²,

2013

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Section: Resultsmentioning

confidence: 99%

Large-scale global identification of protein lysine methylation in vivo

Arnaudo²,

2013

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“…Methylation of proteins and RNAs is a widespread modification known to modulate their functions (42,48,65). Trm112 activates several class I SAM-dependent MTases with substrates implicated in translation, such as several tRNAs (modified by Trm9 and Trm11), and the eukaryotic release factor 1 (by Mtq2).…”

Section: Discussionmentioning

confidence: 99%

Trm112 Is Required for Bud23-Mediated Methylation of the 18S rRNA at Position G1575

Figaro

Wacheul

Schillewaert

et al. 2012

Molecular and Cellular Biology

122

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Posttranscriptional and posttranslational modification of macromolecules is known to fine-tune their functions. Trm112 is unique, acting as an activator of both tRNA and protein methyltransferases. Here we report that in Saccharomyces cerevisiae, Trm112 is required for efficient ribosome synthesis and progression through mitosis. Trm112 copurifies with pre-rRNAs and with multiple ribosome synthesis trans-acting factors, including the 18S rRNA methyltransferase Bud23. Consistent with the known mechanisms of activation of methyltransferases by Trm112, we found that Trm112 interacts directly with Bud23 in vitro and that it is required for its stability in vivo. Consequently, trm112⌬ cells are deficient for Bud23-mediated 18S rRNA methylation at position G1575 and for small ribosome subunit formation. Bud23 failure to bind nascent preribosomes activates a nucleolar surveillance pathway involving the TRAMP complexes, leading to preribosome degradation. Trm112 is thus active in rRNA, tRNA, and translation factor modification, ideally placing it at the interface between ribosome synthesis and function.A ctively growing budding yeast cells produce an average of 33 ribosomes per second, which is considerable (61). Besides the synthesis of its constituents, i.e., 79 ribosomal proteins and 4 rRNAs, ribogenesis involves a large number of so-called transacting factors, including proteins and small nucleolar RNAs (13, 56). These interact only transiently with preribosomes and are required for pre-rRNA processing (i.e., cleavages), pre-rRNA modification, and preribosome assembly and transport.Ribosome synthesis is initiated in the nucleolus, a highly dynamic specialized subcompartment of the nucleus organized around clusters of actively transcribed rRNA genes (60). There, RNA polymerase I produces a 35S/47S (in yeasts and humans, respectively) primary transcript which is processed through a complex succession of endo-and exoribonucleolytic cleavages into three of the four mature rRNAs, the 18S, 5.8S, and 25S/28S rRNAs. The fourth rRNA, 5S, is independently transcribed by RNA polymerase III. Ribosome maturation starts cotranscriptionally in the nucleolus, progresses in the nucleoplasm until preribosomes reach the nuclear pore complex, and is finalized in the cytoplasm. Cytoplasmic maturation steps consisting of pre-rRNA processing and structural reorganization result in the assembly of prominent ribosomal structures, such as the "beak" of the small subunit (SSU) and the "stalk" of the large subunit, and are a prerequisite to the acquisition of functionality (43).It is not clear how the various facets of ribosome synthesis are integrated with ribosome function. However, there is growing evidence that such coordination exists. For the small subunit, recent cryoelectron microscopy (cryo-EM) maps of late pre-40S subunits indicate that the binding of trans-acting factors literally mask functional sites, preventing premature translation initiation (57). For the large subunit, trans-acting factors that resemble ribosomal proteins (suc...

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“…2A, GATA4 was robustly methylated by wild-type PRMT5, but not by PRMT5 mutant, indicating that GATA4 is in fact a good substrate for PRMT5. Previous studies have shown that arginine residues in the RXG motif and the sequences containing proline at either or both of these positions X(P)RXXX(P) were significantly favored to be methylated by arginine methyltransferase (27,28). To pinpoint the PRMT5-mediated methylation sites in GATA4, we examined the protein sequence of GATA4 and identified the arginine residues at positions of 229 (Arg-229), 265 (Arg-265), and 317 (Arg-317) as potential sites (Fig.…”

Section: Prmt5mentioning

confidence: 99%

Inhibition of Cardiomyocyte Hypertrophy by Protein Arginine Methyltransferase 5

Chen

Sun

2014

Journal of Biological Chemistry

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Background: Protein arginine methyltransferase 5 (PRMT5) is a type II protein arginine methyltransferase that catalyzes the symmetrical dimethylation of arginine residues within target proteins. Results: PRMT5 interacts with and methylates GATA4 in cardiomyocytes. Conclusion: PRMT5 suppresses hypertrophic responses in cardiomyocytes by attenuating GATA4 transcriptional activity. Significance: Targeting PRMT5 may represent a novel therapeutic strategy for preventing cardiac hypertrophy and heart failure.

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Identification of arginine- and lysine-methylation in the proteome of Saccharomyces cerevisiae and its functional implications

Cited by 84 publications

References 82 publications

Large-scale global identification of protein lysine methylation in vivo

Large-scale global identification of protein lysine methylation in vivo

Trm112 Is Required for Bud23-Mediated Methylation of the 18S rRNA at Position G1575

Inhibition of Cardiomyocyte Hypertrophy by Protein Arginine Methyltransferase 5

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