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Protein and Mg(2+)-induced conformational changes in the S15 binding site of 16 S ribosomal RNA.
J Mol Biol. 1998 Jan 23; 275(3):453-64.JM

Abstract

The Bacillus stearothermophilus ribosomal protein S15 binds to the central domain of the 16 S rRNA inducing a conformational change in a three-way helical junction. To understand the nature of this conformational change, extended-helical junctions were prepared to examine the effects of S15 or Mg2+ binding on the relative helical orientation using native gel electrophoretic mobility and transient electric birefringence. The free junction is planar with approximately 120 degrees interhelical angles, whereas S15 and Mg2+ yield a junction conformation that remains planar in which two helices, 21 and 22, become colinear and the third, helix 20, forms a 60 degrees angle with respect to helix 22. This conformational change is thought to be important for directing the assembly of the central domain of the 30 S ribosomal subunit.

Authors+Show Affiliations

Department of Chemistry, Massachusetts Institute of Technology, Cambridge 02139, USA.No affiliation info availableNo affiliation info available

Pub Type(s)

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

Language

eng

PubMed ID

9466923

Citation

Orr, J W., et al. "Protein and Mg(2+)-induced Conformational Changes in the S15 Binding Site of 16 S Ribosomal RNA." Journal of Molecular Biology, vol. 275, no. 3, 1998, pp. 453-64.
Orr JW, Hagerman PJ, Williamson JR. Protein and Mg(2+)-induced conformational changes in the S15 binding site of 16 S ribosomal RNA. J Mol Biol. 1998;275(3):453-64.
Orr, J. W., Hagerman, P. J., & Williamson, J. R. (1998). Protein and Mg(2+)-induced conformational changes in the S15 binding site of 16 S ribosomal RNA. Journal of Molecular Biology, 275(3), 453-64.
Orr JW, Hagerman PJ, Williamson JR. Protein and Mg(2+)-induced Conformational Changes in the S15 Binding Site of 16 S Ribosomal RNA. J Mol Biol. 1998 Jan 23;275(3):453-64. PubMed PMID: 9466923.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Protein and Mg(2+)-induced conformational changes in the S15 binding site of 16 S ribosomal RNA. AU - Orr,J W, AU - Hagerman,P J, AU - Williamson,J R, PY - 1998/2/19/pubmed PY - 1998/2/19/medline PY - 1998/2/19/entrez SP - 453 EP - 64 JF - Journal of molecular biology JO - J Mol Biol VL - 275 IS - 3 N2 - The Bacillus stearothermophilus ribosomal protein S15 binds to the central domain of the 16 S rRNA inducing a conformational change in a three-way helical junction. To understand the nature of this conformational change, extended-helical junctions were prepared to examine the effects of S15 or Mg2+ binding on the relative helical orientation using native gel electrophoretic mobility and transient electric birefringence. The free junction is planar with approximately 120 degrees interhelical angles, whereas S15 and Mg2+ yield a junction conformation that remains planar in which two helices, 21 and 22, become colinear and the third, helix 20, forms a 60 degrees angle with respect to helix 22. This conformational change is thought to be important for directing the assembly of the central domain of the 30 S ribosomal subunit. SN - 0022-2836 UR - https://www.unboundmedicine.com/medline/citation/9466923/Protein_and_Mg_2+__induced_conformational_changes_in_the_S15_binding_site_of_16_S_ribosomal_RNA_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0022-2836(97)91489-3 DB - PRIME DP - Unbound Medicine ER -