Nucleic Acids Research, 2000, Vol. 28, No. 3 736-743
© 2000 Oxford University Press
The ribosomal P-proteins of the medfly Ceratitis capitata form a heterogeneous stalk structure interacting with the endogenous P-proteins, in conditional P0-null strains of the yeast Saccharomyces cerevisiae
University of Athens, Department of Biology, Division of Genetics and Biotechnology, Panepistimiopolis, Kouponia, 15701 Athens, Greece and 1Centro de Biologia Molecular Severo Ochoa, CSIC and UAM, Canto Blanco, 28049 Madrid, Spain
The genes encoding the ribosomal P-proteins CcP0, CcP1 and CcP2 of Ceratitis capitata were expressed in the conditional P0-null strains W303dGP0 and D67dGP0 of Saccharomyces cerevisiae, the ribosomes of which contain either standard amounts or are totally deprived of the P1/P2 proteins, respectively. The presence of the CcP0 protein restored cell viability but reduced the growth rate. In the W303CcP0 strain, all four acidic yeast proteins were found on the ribosomes, but in notably less quantity, while a preferable binding of the YP1
/YP2ß pair was established. In the absence of the endogenous P1/P2 proteins in the D67CcP0 strain, the complementation capacity of the CcP0 protein was considerably reduced. The simultaneous expression of the three medfly genes resulted in alterations of the stalk composition: both the CcP1 and CcP2 proteins were found on the particles substituting the YP1 and YP2 proteins, respectively, but their presence did not alter the growth rate, except in the case of the YP1/ß defective strain, where a helping effect on the binding of the YP2 and YP2ß proteins on the ribosomes was confirmed. Therefore, the medfly ribosomal P-proteins complement the yeast P-protein deficient strains forming an heterogeneous ribosomal stalk, which, however, is not functionally equivalent to the endogenous one.
* To whom correspondence should be addressed. Tel: +30 1 72 74 607; Fax: +30 1 72 31 634; Email: skougian@biology.db.uoa.gr
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