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Rat RL23a ribosomal protein efficiently competes with its Saccharomyces cerevisiae L25 homologue for assembly into 60 S subunits.
J Mol Biol. 1996 Nov 15; 263(5):648-56.JM

Abstract

The large subunit protein RL23a from rat liver ribosomes shows 62% sequence identity with the primary rRNA-binding ribosomal protein L25 from Saccharomyces cerevisiae. In vitro binding studies indicated that both r-proteins are able to recognise the L25 binding site on yeast 25 S rRNA and its structural homologue on mammalian 28 S rRNA with equal efficiency. To determine whether the two r-proteins are also functionally equivalent in vivo, a single plasmid-borne copy of either the wild-type L25 gene or the RL23a cDNA, driven by the L25 promoter, was introduced into a yeast strain in which the chromosomal L25 gene is under control of the glucose-repressible GALI-10 promoter. No difference in growth rate could be detected between the two types of transformants when cultured on glucose-based medium. In cells that co-express epitope-tagged versions of L25 and RL23a from single-copy genes, approximately 35% of the 60 S subunits contained the heterologous protein as determined by Western analysis. This value could be increased to 55% by overexpressing RL23a using a multi-copy plasmid. These data demonstrate that rat RL23a can act as a highly efficient substitute for its yeast counterpart in the assembly of functional yeast ribosomes even in the presence of the endogenous L25 protein.

Authors+Show Affiliations

Department of Biochem. and Mol. Biol., IMBW BioCentrum Amsterdam Vrije Universiteit, The Netherlands.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

8947565

Citation

Jeeninga, R E., et al. "Rat RL23a Ribosomal Protein Efficiently Competes With Its Saccharomyces Cerevisiae L25 Homologue for Assembly Into 60 S Subunits." Journal of Molecular Biology, vol. 263, no. 5, 1996, pp. 648-56.
Jeeninga RE, Venema J, Raué HA. Rat RL23a ribosomal protein efficiently competes with its Saccharomyces cerevisiae L25 homologue for assembly into 60 S subunits. J Mol Biol. 1996;263(5):648-56.
Jeeninga, R. E., Venema, J., & Raué, H. A. (1996). Rat RL23a ribosomal protein efficiently competes with its Saccharomyces cerevisiae L25 homologue for assembly into 60 S subunits. Journal of Molecular Biology, 263(5), 648-56.
Jeeninga RE, Venema J, Raué HA. Rat RL23a Ribosomal Protein Efficiently Competes With Its Saccharomyces Cerevisiae L25 Homologue for Assembly Into 60 S Subunits. J Mol Biol. 1996 Nov 15;263(5):648-56. PubMed PMID: 8947565.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Rat RL23a ribosomal protein efficiently competes with its Saccharomyces cerevisiae L25 homologue for assembly into 60 S subunits. AU - Jeeninga,R E, AU - Venema,J, AU - Raué,H A, PY - 1996/11/15/pubmed PY - 1996/11/15/medline PY - 1996/11/15/entrez SP - 648 EP - 56 JF - Journal of molecular biology JO - J Mol Biol VL - 263 IS - 5 N2 - The large subunit protein RL23a from rat liver ribosomes shows 62% sequence identity with the primary rRNA-binding ribosomal protein L25 from Saccharomyces cerevisiae. In vitro binding studies indicated that both r-proteins are able to recognise the L25 binding site on yeast 25 S rRNA and its structural homologue on mammalian 28 S rRNA with equal efficiency. To determine whether the two r-proteins are also functionally equivalent in vivo, a single plasmid-borne copy of either the wild-type L25 gene or the RL23a cDNA, driven by the L25 promoter, was introduced into a yeast strain in which the chromosomal L25 gene is under control of the glucose-repressible GALI-10 promoter. No difference in growth rate could be detected between the two types of transformants when cultured on glucose-based medium. In cells that co-express epitope-tagged versions of L25 and RL23a from single-copy genes, approximately 35% of the 60 S subunits contained the heterologous protein as determined by Western analysis. This value could be increased to 55% by overexpressing RL23a using a multi-copy plasmid. These data demonstrate that rat RL23a can act as a highly efficient substitute for its yeast counterpart in the assembly of functional yeast ribosomes even in the presence of the endogenous L25 protein. SN - 0022-2836 UR - https://www.unboundmedicine.com/medline/citation/8947565/Rat_RL23a_ribosomal_protein_efficiently_competes_with_its_Saccharomyces_cerevisiae_L25_homologue_for_assembly_into_60_S_subunits_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0022-2836(96)90605-1 DB - PRIME DP - Unbound Medicine ER -