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Nucleic Acids Research, 1995, Vol. 23, No. 11 1912-1918
© 1995

MOLECULAR BIOLOGY

gar2 is a nucleolar protein from Schizosaccharomyces pombe required for 18S rRNA and 40S ribosomal subunit accumulation

Marie-Pierre Gulli, Jean-Philippe Girard+,, Dan Zabetakis1, Bruno Lapeyre§,, Teri Melese1 and Michele Caizergues-Ferrer*,

Laboratoire de Biologie Moléculaire Eucaryote du CNRS 118 Route de Narbonne, 31062 Toulouse, France 1Columbia University, Department of Biological Sciences New York, NY, USA

* To whom correspondence should be addressed

Received February 23, 1995. Revised April 27, 1995. Accepted April 27, 1995.

Several nucleolar proteins, such as nucleolin, NOP1/flbrillarln, SSB1, NSR1 and GAR1 share a common glycine and arglnlne rich structural motif called the GAR domain. To identify novel nucleolar proteins from fission yeast we screened Schizosaccharomyces pombe genomic DNA libraries with a probe encompassing the GAR structural motif. Here we report the identification and characterization of a S.pombe gene coding for a novel nucleolar protein, designated gar2. The structure of the fission yeast gar2 is reminiscent of that of nucleolin from vertebrates and NSR1 from Saccharomyces cerevlslae. In addition, like these proteins, gar2 has a nucleolar localisation. The disruption of the gar2+ gene affects normal cell growth, leads to an accumulation of 35S pre-rRNA and a decrease of mature 18S rRNA steady state levels. Moreover, ribosomal profiles of the mutant show an Increase of free 60S ribosomal subuntts and an absence of free 40S ribosomal subunlts. gar2 is able to rescue a S.cerevlslae mutant lacking NSR1, thus establishing gar2 as a functional homolog of NSR1. We propose that gar2 helps the assembly of pre-ribosomal particles containing 18S rRNA.

+Present addresses: The Center for Blood Research, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA

§Division of Biochemistry and Molecular Biology, 401 Barker Hall, University of California at Berkeley, Berkeley, CA 94720, USA


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