Previous Article | Next Article 
Mol Cell Biol. 1990 May; 10(5): 2182-2190
Disruption of single-copy genes encoding acidic ribosomal proteins in Saccharomyces cerevisiae.
M Remacha,
C Santos and
J P Ballesta
Centro de Biologia Molecular, CSIC, Canto Blanco, Madrid, Spain.
ABSTRACT
Using the cloned genes coding for the ribosomal acidic proteins L44 and L45, constructions were made which deleted part of the coding sequence and inserted a DNA fragment at that site carrying either the URA3 or HIS3 gene. By gene disruption techniques with linearized DNA from these constructions, strains of Saccharomyces cerevisiae were obtained which lacked a functional gene for either protein L44 or protein L45. The disrupted genes in the transformants were characterized by Southern blots. The absence of the proteins was verified by electrofocusing and immunological techniques, but a compensating increase of the other acidic ribosomal proteins was not detected. The mutant lacking L44 grew at a rate identical to the parental strain in complex as well as in minimal medium. The L45-disrupted strain also grew well in both media but at a slower rate than the parental culture. A diploid strain was obtained by crossing both transformants, and by tetrad analysis it was shown that the double transformant lacking both genes is not viable. These results indicated that proteins L44 and L45 are independently dispensable for cell growth and that the ribosome is functional in the absence of either of them.
Mol Cell Biol. 1990 May; 10(5): 2182-2190
This article has been cited by other articles:
-
Grela, P., Sawa-Makarska, J., Gordiyenko, Y., Robinson, C. V., Grankowski, N., Tchorzewski, M.
(2008). Structural Properties of the Human Acidic Ribosomal P Proteins Forming the P1-P2 Heterocomplex. J Biochem
143: 169-177
[Abstract]
[Full Text]
-
Rodriguez-Gabriel, M. A., Remacha, M., Ballesta, J. P. G.
(2000). The RNA Interacting Domain but Not the Protein Interacting Domain Is Highly Conserved in Ribosomal Protein P0. J. Biol. Chem.
275: 2130-2136
[Abstract]
[Full Text]
-
Briones, E., Briones, C., Remacha, M., Ballesta, J. P. G.
(1998). The GTPase Center Protein L12 Is Required for Correct Ribosomal Stalk Assembly but Not for Saccharomyces cerevisiae Viability. J. Biol. Chem.
273: 31956-31961
[Abstract]
[Full Text]
-
Szick, K., Springer, M., Bailey-Serres, J.
(1998). Evolutionary analyses of the 12-kDa acidic ribosomal P-proteins reveal a distinct protein of higher plant ribosomes. Proc. Natl. Acad. Sci. USA
95: 2378-2383
[Abstract]
[Full Text]
-
Aguilar, R., Montoya, L., Sánchez de Jiménez, E.
(1998). Synthesis and Phosphorylation of Maize Acidic Ribosomal Proteins . Implications in Translational Regulation. Plant Physiol.
116: 379-385
[Abstract]
[Full Text]
-
Santos, C., Ballesta, J. P. G.
(1995). The Highly Conserved Protein P0 Carboxyl End Is Essential for Ribosome Activity Only in the Absence of Proteins P1 and P2. J. Biol. Chem.
270: 20608-20614
[Abstract]
[Full Text]
-
Szick-Miranda, K., Bailey-Serres, J.
(2001). Regulated Heterogeneity in 12-kDa P-protein Phosphorylation and Composition of Ribosomes in Maize (Zea mays L.). J. Biol. Chem.
276: 10921-10928
[Abstract]
[Full Text]
Copyright © 1990 by the American Society for Microbiology. All rights reserved.