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Vol. 9, Issue 8, 2011-2023, August 1998
Laboratoire de Biologie Moleculaire Eucaryote du Centre
National de la Recherche Scientifique, 31062 Toulouse Cedex, France
Nonribosomal nucleolar protein gar2 is required for 18S rRNA and
40S ribosomal subunit production in Schizosaccharomyces
pombe. We have investigated the consequences of the absence of
each structural domain of gar2 on cell growth, 18S rRNA production, and
nucleolar structure. Deletion of gar2 RNA-binding domains (RBDs) causes stronger inhibition of growth and 18S rRNA accumulation than the absence of the whole protein, suggesting that other factors may be
titrated by its remaining N-terminal basic/acidic serine-rich domain.
These drastic functional defects correlate with striking nucleolar
hypertrophy. Point mutations in the conserved RNP1 motifs of gar2 RBDs
supposed to inhibit RNA-protein interactions are sufficient to induce
severe nucleolar modifications but only in the presence of the
N-terminal domain of the protein. Gar2 and its mutants also distribute
differently in glycerol gradients: gar2 lacking its RBDs is found
either free or assembled into significantly larger complexes than the
wild-type protein. We propose that gar2 helps the assembly on rRNA of
factors necessary for 40S subunit synthesis by providing a physical
link between them. These factors may be recruited by the N-terminal
domain of gar2 and may not be released if interaction of gar2 with rRNA
is impaired.
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