Molecular Genetics and Genomics

, Volume 266, Issue 3, pp 454–462

Ria1p (Ynl163c), a protein similar to elongation factors 2, is involved in the biogenesis of the 60S subunit of the ribosome in Saccharomyces cerevisiae

  •  A.-M. Bécam
  •  F. Nasr
  •  W. Racki
  •  M. Zagulski
  •  C. Herbert
Original Paper

DOI: 10.1007/s004380100548

Cite this article as:
Bécam, AM., Nasr, F., Racki, W. et al. Mol Gen Genomics (2001) 266: 454. doi:10.1007/s004380100548

Abstract.

RIA1 (YNL163c) is a quasi-essential gene that encodes a protein with strong similarities to elongation factors 2. Small C-terminal deletions in the protein lead to a severe growth defect. In the case of a 22-residue C-terminal deletion this can be suppressed by intragenic mutations in the RIA1 gene or dominant extragenic mutations in TIF6, which is thought to be involved in the biogenesis of the 60S subunit of the ribosome. The dominant TIF6 alleles can also suppress the phenotype associated with a complete deletion of the RIA1 gene. Depletion of Ria1p has a dramatic effect on the polysome profile: there is a severe reduction in the level of the 80S monosomes, an imbalance in the 40S/60S ratio, and halfmers appear. Dissociation of the monosomes and polysomes in the Ria1p depletion mutant revealed a specific reduction in the amount of 60S subunits. Localization experiments with HA-tagged derivatives of Ria1p did not detect any stable association of Ria1p with ribosome subunits, 80S monosomes or polysomes. Cell fractionation experiments show that Ria1p is found in both the cytoplasmic fraction and the nuclear fraction. Taken together, these data suggest that Ria1p is involved in the biogenesis of the 60S subunit of the ribosome.

Ria1p Tif6p Elongation factor 2 60S ribosome subunit Saccharomyces cerevisiae 

Copyright information

© Springer-Verlag 2001

Authors and Affiliations

  •  A.-M. Bécam
    • 1
  •  F. Nasr
    • 1
  •  W. Racki
    • 1
  •  M. Zagulski
    • 1
  •  C. Herbert
    • 1
  1. 1.Centre de Génétique Moléculaire du CNRS, associé à l'Université Pierre et Marie Curie, F-91198 Gif-sur-Yvette, France
  2. 2.Present address: Département des Sciences Naturelles, Faculté des Sciences, Section I, Université Libanaise, Hadath-Beyrouth, Lebanon
  3. 3.Present address: Institute of Biochemistry and Biophysics, Polish National Academy of Sciences, 5a Pawinskiego, 02-106, Warsaw, Poland

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