A novel SET domain methyltransferase in yeast: Rkm2-dependent trimethylation of ribosomal protein L12ab at lysine 10.

A novel SET domain methyltransferase in yeast: Rkm2-dependent trimethylation of ribosomal protein L12ab at lysine 10. Research Abstract Details 

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A novel SET domain methyltransferase in yeast: Rkm2-dependent trimethylation of ribosomal protein L12ab at lysine 10. Abstract Text:

Tanya R Porras-Yakushi,Julian P Whitelegge,Steven Clarke,

The ribosomal protein L12ab (Rpl12ab) in Saccharomyces cerevisiae is modified by methylation at both arginine and lysine residues. Although the enzyme responsible for the modification reaction at arginine 66 has been identified (Rmt2), the enzyme(s) responsible for the lysine modification(s) has not been found, and the site(s) of methylation has not been determined. Here we demonstrate, using a combination of mass spectrometry and labeling assays, that the yeast gene YDR198c encodes the enzyme responsible for the predominant epsilon-trimethylation at lysine 10 in Rpl12ab. An additional site of predominant epsilon-dimethylation is observed at lysine 3; the enzyme catalyzing this modification is not known. The YDR198c gene encodes a SET domain similar to that of the Rkm1 enzyme responsible for modifying Rpl23ab, and we have now designated the YDR198c gene product as Rkm2 (ribosomal lysine methyltransferase 2). The effect of the loss of the enzyme on ribosomal complex stability was studied by polysomal fractionation. However, no difference was observed between the Deltarkm2 deletion strain and its parent wild type strain. With the identification of this enzyme, it appears that the 12 SET domain family members in yeast can now be divided into two subfamilies based on function and amino acid sequence identity. One branch includes enzymes that modify histones, including Set1 and Set2; the other branch includes Rkm1, Rkm2, and Ctm1, the cytochrome c methyltransferase. These studies suggest that the remaining seven SET domain proteins may also be lysine methyltransferases.

A novel SET domain methyltransferase in yeast: Rkm2-dependent trimethylation of ribosomal protein L12ab at lysine 10. Publishing Authors By Initials

TR Porras-Yakushi,JP Whitelegge,S Clarke,

For similar proteins: fungal proteins: saccharomyces cerevisiae proteins research abstracts see: proteins: fungal proteins: saccharomyces cerevisiae proteins research

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A novel SET domain methyltransferase in yeast: Rkm2-dependent trimethylation of ribosomal protein L12ab at lysine 10. Journal Published:

PUBLICATION TYPE: Research Support, N.I.H., Extr

Journal: The Journal of biological chemistry

VOLUME: 281

Page Numbers: 35835-45

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 27

MONTH: 09

YEAR: 2006

A novel SET domain methyltransferase in yeast: Rkm2-dependent trimethylation of ribosomal protein L12ab at lysine 10. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 2985121

A novel SET domain methyltransferase in yeast: Rkm2-dependent trimethylation of ribosomal protein L12ab at lysine 10. Keywords Mesh Terms:

KEYWORDS: Saccharomyces cerevisiae Proteins

MESH TERMS: physiology

Chemical & Substance for Abstract: A novel SET domain methyltransferase in yeast: Rkm2-dependent trimethylation of ribosomal protein L12ab at lysine 10. Information

Substance Name: Rkm2 protein, S cerevisiae

Registry Number: EC 2.1.1.43

Grant and Affiliation Information for A novel SET domain methyltransferase in yeast: Rkm2-dependent trimethylation of ribosomal protein L12ab at lysine 10.

AFFILIATION: Department of Chemistry and Biochemistry, Molecular Biology Institute, UCLA, Los Angeles, California 90095-1569, USA.

Country: United States

AGENCY: United States NIGMS

GRANT: GM075381

ACRONYM: GM

MEDLINETA: J Biol Chem

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