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Molecular and Cellular Biology, December 2005, p. 10419-10432, Vol. 25, No. 23
0270-7306/05/$08.00+0     doi:10.1128/MCB.25.23.10419-10432.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Ytm1, Nop7, and Erb1 Form a Complex Necessary for Maturation of Yeast 66S Preribosomes

Tiffany D. Miles, Jelena Jakovljevic, Edward W. Horsey, Piyanun Harnpicharnchai, Lan Tang, and John L. Woolford Jr^*

Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213

Received 2 March 2005/ Returned for modification 29 March 2005/ Accepted 20 September 2005

The essential, conserved yeast nucleolar protein Ytm1 is one of 17 proteins in ribosome assembly intermediates that contain WD40 protein-protein interaction motifs. Such proteins may play key roles in organizing other molecules necessary for ribosome biogenesis. Ytm1 is present in four consecutive 66S preribosomes containing 27SA₂, 27SA₃, 27SB, and 25.5S plus 7S pre-rRNAs plus ribosome assembly factors and ribosomal proteins. Ytm1 binds directly to Erb1 and is present in a heterotrimeric subcomplex together with Erb1 and Nop7, both within preribosomes and independently of preribosomes. However, Nop7 and Erb1 assemble into preribosomes prior to Ytm1. Mutations in the WD40 motifs of Ytm1 disrupt binding to Erb1, destabilize the heterotrimer, and delay pre-rRNA processing and nuclear export of preribosomes. Nevertheless, 66S preribosomes lacking Ytm1 remain otherwise intact.

Present address: Department of Chemical Engineering, Carnegie Mellon University, 700 Technology Drive, PTC Room 4305, Pittsburgh, PA 15219.

Present address: National Center for Genetic Engineering and Biotechnology, Thailand Science Park, 113 Paholyothin Road, Klong 1, Klong Luang, Pathumthani 12120, Thailand.

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