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Nucleic Acids Research, 2003, Vol. 31, No. 10 2524-2533
© 2003 Oxford University Press

RRP20, a component of the 90S preribosome, is required for pre-18S rRNA processing in Saccharomyces cerevisiae

Saengchan Senapin, G. Desmond Clark-Walker, Xin Jie Chen1, Bertrand Séraphin2 and Marie-Claire Daugeron2

Molecular Genetics and Evolution Group, Research School of Biological Sciences, The Australian National University, GPO Box 475, Canberra ACT 2601, Australia, 1 School of Biological Sciences, Nanyang Technological University, Nanyang Walk, Singapore 637616 and 2 Centre de Génétique Moléculaire, CNRS, 1 Avenue de la Terrasse 91190 Gif sur Yvette, France

*To whom correspondence should be addressed. Tel: +33 1 69 82 38 83; Fax: +33 1 69 82 38 77; Email: daugeron{at}cgm.cnrs-gif.fr

A strain of Saccharomyces cerevisiae, defective in small subunit ribosomal RNA processing, has a mutation in YOR145c ORF that converts Gly235 to Asp. Yor145c is a nucleolar protein required for cell viability and has been reported recently to be present in 90S pre-ribosomal particles. The Gly235Asp mutation in YOR145c is found in a KH-type RNA-binding domain and causes a marked deficiency in 18S rRNA production. Detailed studies by northern blotting and primer extension analyses show that the mutant strain impairs the early pre-rRNA processing cleavage essentially at sites A1 and A2, leading to accumulation of a 22S dead-end processing product that is found in only a few rRNA processing mutants. Furthermore, U3, U14, snR10 and snR30 snoRNAs, involved in early pre-rRNA cleavages, are not destabilized by the YOR145c mutation. As the protein encoded by YOR145c is found in pre-ribosomal particles and the mutant strain is defective in ribosomal RNA processing, we have renamed it as RRP20.


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