ArticleProtein science : a publication of the Protein Society2007
Expression of proteins with dimethylarginines in Escherichia coli for protein-protein interaction studies.
Article in Protein science : a publication of the Protein Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed, 16 citations in OpenAlex.
- Global analysis of protein arginine methylation.Cell reports methods · 2021Article
- Arginine methylation augments Sbp1 function in translation repression and decapping.The FEBS journal · 2019Article
- Sbp1 modulates the translation of Pab1 mRNA in a poly(A)- and RGG-dependent manner.RNA (New York, N.Y.) · 2018Article
- Interactions between RNA-binding proteins and P32 homologues in trypanosomes and human cells.Current genetics · 2016Article
- Enhanced methylarginine characterization by post-translational modification-specific targeted data acquisition and electron-transfer dissociation mass spectrometry.Journal of the American Society for Mass Spectrometry · 2012Article
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7 authors at 3 institutions in 1 country.
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Abstract
Protein arginine methylation often modulates protein-protein interactions. To isolate a sufficient quantity of proteins enriched in methyl arginine(s) from natural sources for biochemical studies is laborious and difficult. We describe here an expression system that produces recombinant proteins that are enriched in omega-N(G),N(G)-asymmetry dimethylarginines. A yeast type I arginine methyltransferase gene (HMT1) is put on a plasmid under the control of the Escherichia coli methionine aminopeptidase promoter for constitutive expression. The protein targeted for post-translational modification is put on the same plasmid behind a T7 promoter for inducible expression of His(6)-tagged proteins. Sbp1p and Stm1p were used as model proteins to examine this expression system. The 13 arginines within the arginine-glycine-rich motif of Sbp1p and the RGG sequence near the C terminus of Stm1p were methylated. Unexpectedly, the arginine residue on the thrombin cleavage site (LVPRGS) of the fusion proteins can also be methylated by Hmt1p. Sbp1p and Sbp1p/hmt1 were covalently attached to solid supports for the isolation of interacting proteins. The results indicate that arginine methylation on Sbp1p exerts both positive and negative effects on protein-protein interaction.
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