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Molecular and Cellular Biology, March 1999, p. 2142-2154, Vol. 19, No. 3
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Pseudouridine Mapping in the Saccharomyces cerevisiae Spliceosomal U Small Nuclear RNAs (snRNAs) Reveals that Pseudouridine Synthase Pus1p Exhibits a Dual Substrate Specificity for U2 snRNA and tRNA

Séverine Massenet,1 Yuri Motorin,2 Denis L. J. Lafontaine,3 Eduard C. Hurt,4 Henri Grosjean,2 and Christiane Branlant1,*

Laboratoire de Maturation des ARN et Enzymologie Moléculaire, UMR7567 CNRS-UHP, Faculté des Sciences, 54506 Vandoeuvre-les-Nancy Cédex,1 and Laboratoire d'Enzymologie et Biochimie Structurales, UPR CNRS, 91198 Gif-sur-Yvette,2 France; Institute of Cell and Molecular Biology, University of Edinburgh, Edinburgh EH9 3JR, United Kingdom3; and University of Heidelberg, 69120 Heidelberg, Germany4

Received 24 August 1998/Returned for modification 5 October 1998/Accepted 30 November 1998

Pseudouridine (Psi ) residues were localized in the Saccharomyces cerevisiae spliceosomal U small nuclear RNAs (UsnRNAs) by using the chemical mapping method. In contrast to vertebrate UsnRNAs, S. cerevisiae UsnRNAs contain only a few Psi  residues, which are located in segments involved in intermolecular RNA-RNA or RNA-protein interactions. At these positions, UsnRNAs are universally modified. When yeast mutants disrupted for one of the several pseudouridine synthase genes (PUS1, PUS2, PUS3, and PUS4) or depleted in rRNA-pseudouridine synthase Cbf5p were tested for UsnRNA Psi  content, only the loss of the Pus1p activity was found to affect Psi  formation in spliceosomal UsnRNAs. Indeed, Psi 44 formation in U2 snRNA was abolished. By using purified Pus1p enzyme and in vitro-produced U2 snRNA, Pus1p is shown here to catalyze Psi 44 formation in the S. cerevisiae U2 snRNA. Thus, Pus1p is the first UsnRNA pseudouridine synthase characterized so far which exhibits a dual substrate specificity, acting on both tRNAs and U2 snRNA. As depletion of rRNA-pseudouridine synthase Cbf5p had no effect on UsnRNA Psi  content, formation of Psi  residues in S. cerevisiae UsnRNAs is not dependent on the Cbf5p-snoRNA guided mechanism.

* Corresponding author. Mailing address: Laboratoire de Maturation des ARN et Enzymologie Moléculaire, UMR7567 CNRS-UHP Nancy I, Faculté des Sciences, BP 239, 54506 Vandoeuvre-les-Nancy Cédex, France. Phone: 33-3-83-91-20-92. Fax: 33-3-83-91-20-93. E-mail: cbranlant{at}scbim.u-nancy.fr.

Molecular and Cellular Biology, March 1999, p. 2142-2154, Vol. 19, No. 3
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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