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The Yeast Ribosome Synthesis Factor Emg1 is a Novel Member of the Superfamily of Alpha/beta Knot Fold Methyltransferases

Overview
Journal Nucleic Acids Res
Publisher Oxford University Press
Specialty Biochemistry
Date 2007 Dec 8
PMID 18063569
Citations 37
Authors
Nicolas Leulliot
Markus T Bohnsack
Marc Graille
David Tollervey
Herman Van Tilbeurgh
Affiliations
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Abstract

Emg1 was previously shown to be required for maturation of the 18S rRNA and biogenesis of the 40S ribosomal subunit. Here we report the determination of the crystal structure of Emg1 at 2 A resolution in complex with the methyl donor, S-adenosyl-methionine (SAM). This structure identifies Emg1 as a novel member of the alpha/beta knot fold methyltransferase (SPOUT) superfamily. In addition to the conserved SPOUT core, Emg1 has two unique domains that form an extended surface, which we predict to be involved in binding of RNA substrates. A point mutation within a basic patch on this surface almost completely abolished RNA binding in vitro. Three point mutations designed to disrupt the interaction of Emg1 with SAM each caused>100-fold reduction in SAM binding in vitro. Expression of only Emg1 with these mutations could support growth and apparently normal ribosome biogenesis in strains genetically depleted of Emg1. We conclude that the catalytic activity of Emg1 is not essential and that the presence of the protein is both necessary and sufficient for ribosome biogenesis.

Citing Articles

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The yeast RNA methylation complex consists of conserved yet reconfigured components with m6A-dependent and independent roles.

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Quality control ensures fidelity in ribosome assembly and cellular health.

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Structure Characterization of Pseudouridine Kinase PsuK.

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The epitranscriptome beyond mA.

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