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Contributions of multiple basic amino acids in the C-terminal region of yeast ribosomal protein L1 to 5 S rRNA binding and 60 S ribosome stability.
J Mol Biol. 1995 Feb 17; 246(2):295-307.JM

Abstract

Previous studies suggest that the C-terminal region of ribosomal protein L1 from Saccharomyces cerevisiae is important for its interaction with the 5 S rRNA molecule. Within this region are several highly conserved basic amino acids including Lys276, Lys279, Lys289, Arg282, Arg285. To examine potential contributions of these amino acids to RNA-protein interaction and ribosomal assembly, effects of substitutions of these residues by methionine either individually or in combinations were examined. A methionine substitution of any one of the lysine residues did not significantly affect RNA binding in vitro. The mutant RNPs were as stable as the wild-type RNP. Yeast transformants expressing these mutant proteins grew at the same rate as the wild-type. However, mutant proteins containing substitutions of any two of these basic amino acids bound RNA weakly. The resultant RNPs were significantly less stable than the wild-type. Whereas cells expressing mutant L1 with a single substitution at 289 was not lethal, cells expressing mutant L1 with any double substitutions involving Lys289 as one of the substituted amino acids were lethal. These data suggest that Lys289 plays a key role in the binding of ribosomal protein L1 to 5 S rRNA. The other basic residues, particularly Arg282, and Arg285, in this region also contribute to RNA binding. These residues are predicted to locate on the same side of an alpha helix. We would like to propose a structural model for the yeast RNP that involves multiple contact sites located on one side of the helix in the C terminus of the protein and the 5 S rRNA. These basic amino acids also participate, directly or indirectly, in the interaction of the RNP complex with other components of the 60 S ribosomal subunit.

Authors+Show Affiliations

Department of Biochemistry, University of Texas Health Science Center at San Antonio 78284.No affiliation info available

Pub Type(s)

Comparative Study
Journal Article
Research Support, U.S. Gov't, P.H.S.

Language

eng

PubMed ID

7869381

Citation

Yeh, L C., and J C. Lee. "Contributions of Multiple Basic Amino Acids in the C-terminal Region of Yeast Ribosomal Protein L1 to 5 S rRNA Binding and 60 S Ribosome Stability." Journal of Molecular Biology, vol. 246, no. 2, 1995, pp. 295-307.
Yeh LC, Lee JC. Contributions of multiple basic amino acids in the C-terminal region of yeast ribosomal protein L1 to 5 S rRNA binding and 60 S ribosome stability. J Mol Biol. 1995;246(2):295-307.
Yeh, L. C., & Lee, J. C. (1995). Contributions of multiple basic amino acids in the C-terminal region of yeast ribosomal protein L1 to 5 S rRNA binding and 60 S ribosome stability. Journal of Molecular Biology, 246(2), 295-307.
Yeh LC, Lee JC. Contributions of Multiple Basic Amino Acids in the C-terminal Region of Yeast Ribosomal Protein L1 to 5 S rRNA Binding and 60 S Ribosome Stability. J Mol Biol. 1995 Feb 17;246(2):295-307. PubMed PMID: 7869381.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Contributions of multiple basic amino acids in the C-terminal region of yeast ribosomal protein L1 to 5 S rRNA binding and 60 S ribosome stability. AU - Yeh,L C, AU - Lee,J C, PY - 1995/2/17/pubmed PY - 1995/2/17/medline PY - 1995/2/17/entrez SP - 295 EP - 307 JF - Journal of molecular biology JO - J Mol Biol VL - 246 IS - 2 N2 - Previous studies suggest that the C-terminal region of ribosomal protein L1 from Saccharomyces cerevisiae is important for its interaction with the 5 S rRNA molecule. Within this region are several highly conserved basic amino acids including Lys276, Lys279, Lys289, Arg282, Arg285. To examine potential contributions of these amino acids to RNA-protein interaction and ribosomal assembly, effects of substitutions of these residues by methionine either individually or in combinations were examined. A methionine substitution of any one of the lysine residues did not significantly affect RNA binding in vitro. The mutant RNPs were as stable as the wild-type RNP. Yeast transformants expressing these mutant proteins grew at the same rate as the wild-type. However, mutant proteins containing substitutions of any two of these basic amino acids bound RNA weakly. The resultant RNPs were significantly less stable than the wild-type. Whereas cells expressing mutant L1 with a single substitution at 289 was not lethal, cells expressing mutant L1 with any double substitutions involving Lys289 as one of the substituted amino acids were lethal. These data suggest that Lys289 plays a key role in the binding of ribosomal protein L1 to 5 S rRNA. The other basic residues, particularly Arg282, and Arg285, in this region also contribute to RNA binding. These residues are predicted to locate on the same side of an alpha helix. We would like to propose a structural model for the yeast RNP that involves multiple contact sites located on one side of the helix in the C terminus of the protein and the 5 S rRNA. These basic amino acids also participate, directly or indirectly, in the interaction of the RNP complex with other components of the 60 S ribosomal subunit. SN - 0022-2836 UR - https://www.unboundmedicine.com/medline/citation/7869381/Contributions_of_multiple_basic_amino_acids_in_the_C_terminal_region_of_yeast_ribosomal_protein_L1_to_5_S_rRNA_binding_and_60_S_ribosome_stability_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0022-2836(84)70085-4 DB - PRIME DP - Unbound Medicine ER -