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Molecular and Cellular Biology, May 2008, p. 3089-3100, Vol. 28, No. 10
0270-7306/08/$08.00+0     doi:10.1128/MCB.01574-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Different Mechanisms for Pseudouridine Formation in Yeast 5S and 5.8S rRNAs{triangledown}

Wayne A. Decatur1* and Murray N. Schnare2

Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, Massachusetts 01003,1 Department of Biochemistry and Molecular Biology, Dalhousie University, Halifax, Nova Scotia B3H 1X5, Canada2

Received 27 August 2007/ Returned for modification 23 October 2007/ Accepted 26 February 2008

The selection of sites for pseudouridylation in eukaryotic cytoplasmic rRNA occurs by the base pairing of the rRNA with specific guide sequences within the RNA components of box H/ACA small nucleolar ribonucleoproteins (snoRNPs). Forty-four of the 46 pseudouridines ({Psi}s) in the cytoplasmic rRNA of Saccharomyces cerevisiae have been assigned to guide snoRNAs. Here, we examine the mechanism of {Psi} formation in 5S and 5.8S rRNA in which the unassigned {Psi}s occur. We show that while the formation of the {Psi} in 5.8S rRNA is associated with snoRNP activity, the pseudouridylation of 5S rRNA is not. The position of the {Psi} in 5.8S rRNA is guided by snoRNA snR43 by using conserved sequence elements that also function to guide pseudouridylation elsewhere in the large-subunit rRNA; an internal stem-loop that is not part of typical yeast snoRNAs also is conserved in snR43. The multisubstrate synthase Pus7 catalyzes the formation of the {Psi} in 5S rRNA at a site that conforms to the 7-nucleotide consensus sequence present in other substrates of Pus7. The different mechanisms involved in 5S and 5.8S rRNA pseudouridylation, as well as the multiple specificities of the individual trans factors concerned, suggest possible roles in linking ribosome production to other processes, such as splicing and tRNA synthesis.

* Corresponding author. Mailing address: Department of Biochemistry and Molecular Biology, 903 Lederle Graduate Research Tower, University of Massachusetts, Amherst, MA 01003. Phone: (413) 545-0566. Fax: (413) 545-3291. E-mail: wdecatur{at}biochem.umass.edu

{triangledown} Published ahead of print on 10 March 2008.

Molecular and Cellular Biology, May 2008, p. 3089-3100, Vol. 28, No. 10
0270-7306/08/$08.00+0     doi:10.1128/MCB.01574-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Muller, S., Urban, A., Hecker, A., Leclerc, F., Branlant, C., Motorin, Y. (2009). Deficiency of the tRNATyr:{Psi}35-synthase aPus7 in Archaea of the Sulfolobales order might be rescued by the H/ACA sRNA-guided machinery. Nucleic Acids Res 37: 1308-1322 [Abstract] [Full Text]  
  • Urban, A., Behm-Ansmant, I., Branlant, C., Motorin, Y. (2009). RNA Sequence and Two-dimensional Structure Features Required for Efficient Substrate Modification by the Saccharomyces cerevisiae RNA:{Psi}-Synthase Pus7p. J. Biol. Chem. 284: 5845-5858 [Abstract] [Full Text]  


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