Abstract
Analysis of the Haloarcula marismortui large ribosomal subunit has revealed a common RNA structure that we call the kink-turn, or K-turn. The six K-turns in H.marismortui 23S rRNA superimpose with an r.m.s.d. of 1.7 A. There are two K-turns in the structure of Thermus thermophilus 16S rRNA, and the structures of U4 snRNA and L30e mRNA fragments form K-turns. The structure has a kink in the phosphodiester backbone that causes a sharp turn in the RNA helix. Its asymmetric internal loop is flanked by C-G base pairs on one side and sheared G-A base pairs on the other, with an A-minor interaction between these two helical stems. A derived consensus secondary structure for the K-turn includes 10 consensus nucleotides out of 15, and predicts its presence in the 5'-UTR of L10 mRNA, helix 78 in Escherichia coli 23S rRNA and human RNase MRP. Five K-turns in 23S rRNA interact with nine proteins. While the observed K-turns interact with proteins of unrelated structures in different ways, they interact with L7Ae and two homologous proteins in the same way.
MeSH Terms
Amino Acid Sequence
DNA
Haloarcula marismortui/genetics
Helix-Loop-Helix Motifs
Models, Molecular
Molecular Sequence Data
Nucleic Acid Conformation
RNA, Archaeal/chemistry,metabolism
RNA, Ribosomal/chemistry,metabolism
Ribosomal Proteins/metabolism
Chemicals
RNA, Archaeal
RNA, Ribosomal
Ribosomal Proteins
kinked DNA
DNA
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Klein D J
Department of Molecular Biophysics and Biochemistry, Yale University and Howard Hughes Medical Institute, New Haven, CT 06520-8114, USA.
Schmeing T M
Moore P B
Steitz T A
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