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The phylogenetically conserved doublet tertiary interaction in domain III of the large subunit rRNA is crucial for ribosomal protein binding.
Proc Natl Acad Sci U S A. 1993 Jan 01; 90(1):213-6.PN

Abstract

Previous phylogenetic analysis of rRNA sequences for covariant base changes has identified approximately 20 potential tertiary interactions. One of these is present in domain III of the large subunit rRNA and consists of two adjacent Watson-Crick base pairs that, in Saccharomyces cerevisiae 26S rRNA, connect positions 1523 and 1524 to positions 1611 and 1612. This interaction would strongly affect the structure of an evolutionarily highly conserved region that acts as the binding site for the early-assembling ribosomal proteins L25 and EL23 of S. cerevisiae and Escherichia coli, respectively. To assess the functional importance of this tertiary interaction, we determined the ability of synthetically prepared S. cerevisiae ribosomal protein L25 to associate in vitro with synthetic 26S rRNA fragments containing sequence variations at positions 1523 and 1524 and/or positions 1611 and 1612. Mutations that prevent the formation of both base pairs abolished L25 binding completely, whereas the introduction of compensatory mutations fully restored protein binding. Disruption of only the U1524.A1611 pair reduced L25 binding to approximately 30% of the value shown by the wild-type 26S rRNA fragment, whereas disruption of the G1523.C1612 base pair resulted in almost complete loss of protein binding. These results strongly support the existence and functional importance of the proposed doublet tertiary interaction in domain III of the large subunit rRNA.

Authors+Show Affiliations

Department of Biochemistry and Molecular Biology, Faculty of Chemistry, Vrije Universiteit, Amsterdam, The Netherlands.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

8419926

Citation

Kooi, E A., et al. "The Phylogenetically Conserved Doublet Tertiary Interaction in Domain III of the Large Subunit rRNA Is Crucial for Ribosomal Protein Binding." Proceedings of the National Academy of Sciences of the United States of America, vol. 90, no. 1, 1993, pp. 213-6.
Kooi EA, Rutgers CA, Mulder A, et al. The phylogenetically conserved doublet tertiary interaction in domain III of the large subunit rRNA is crucial for ribosomal protein binding. Proc Natl Acad Sci U S A. 1993;90(1):213-6.
Kooi, E. A., Rutgers, C. A., Mulder, A., Van't Riet, J., Venema, J., & Raué, H. A. (1993). The phylogenetically conserved doublet tertiary interaction in domain III of the large subunit rRNA is crucial for ribosomal protein binding. Proceedings of the National Academy of Sciences of the United States of America, 90(1), 213-6.
Kooi EA, et al. The Phylogenetically Conserved Doublet Tertiary Interaction in Domain III of the Large Subunit rRNA Is Crucial for Ribosomal Protein Binding. Proc Natl Acad Sci U S A. 1993 Jan 1;90(1):213-6. PubMed PMID: 8419926.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The phylogenetically conserved doublet tertiary interaction in domain III of the large subunit rRNA is crucial for ribosomal protein binding. AU - Kooi,E A, AU - Rutgers,C A, AU - Mulder,A, AU - Van't Riet,J, AU - Venema,J, AU - Raué,H A, PY - 1993/1/1/pubmed PY - 1993/1/1/medline PY - 1993/1/1/entrez SP - 213 EP - 6 JF - Proceedings of the National Academy of Sciences of the United States of America JO - Proc Natl Acad Sci U S A VL - 90 IS - 1 N2 - Previous phylogenetic analysis of rRNA sequences for covariant base changes has identified approximately 20 potential tertiary interactions. One of these is present in domain III of the large subunit rRNA and consists of two adjacent Watson-Crick base pairs that, in Saccharomyces cerevisiae 26S rRNA, connect positions 1523 and 1524 to positions 1611 and 1612. This interaction would strongly affect the structure of an evolutionarily highly conserved region that acts as the binding site for the early-assembling ribosomal proteins L25 and EL23 of S. cerevisiae and Escherichia coli, respectively. To assess the functional importance of this tertiary interaction, we determined the ability of synthetically prepared S. cerevisiae ribosomal protein L25 to associate in vitro with synthetic 26S rRNA fragments containing sequence variations at positions 1523 and 1524 and/or positions 1611 and 1612. Mutations that prevent the formation of both base pairs abolished L25 binding completely, whereas the introduction of compensatory mutations fully restored protein binding. Disruption of only the U1524.A1611 pair reduced L25 binding to approximately 30% of the value shown by the wild-type 26S rRNA fragment, whereas disruption of the G1523.C1612 base pair resulted in almost complete loss of protein binding. These results strongly support the existence and functional importance of the proposed doublet tertiary interaction in domain III of the large subunit rRNA. SN - 0027-8424 UR - https://www.unboundmedicine.com/medline/citation/8419926/The_phylogenetically_conserved_doublet_tertiary_interaction_in_domain_III_of_the_large_subunit_rRNA_is_crucial_for_ribosomal_protein_binding_ L2 - http://www.pnas.org/cgi/pmidlookup?view=long&pmid=8419926 DB - PRIME DP - Unbound Medicine ER -