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Nucleic Acids Research Advance Access originally published online on December 6, 2007
Nucleic Acids Research 2008 36(2):629-639; doi:10.1093/nar/gkm1074
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Nucleic Acids Research, 2008, Vol. 36, No. 2 629-639
© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Nucleic Acid Enzymes

The yeast ribosome synthesis factor Emg1 is a novel member of the superfamily of alpha/beta knot fold methyltransferases

Nicolas Leulliot1,*, Markus T. Bohnsack2, Marc Graille1, David Tollervey2 and Herman Van Tilbeurgh1

1Institut de Biochimie et de Biophysique Moléculaire et Cellulaire, UMR8619, Bât 430, Université de Paris-Sud, 91405 Orsay Cedex, France and 2Wellcome Trust Centre for Cell Biology, University of Edinburgh, EH9 3JR, UK

*To whom correspondence should be addressed. Tel: 33 169155047; Fax: 33 169853715; Email: nicolas.leulliot{at}u-psud.fr

Received October 10, 2007. Revised November 12, 2007. Accepted November 14, 2007.

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 Å 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.

The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors.


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