High-resolution Proton Magnetic Resonance Study of the Secondary Structure of the 3'-terminal 49-nucleotide Fragment of 16S RRNA from Escherichia Coli

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1977 Mar 1

PMID 322143

Citations 20

Authors

R A Baan

C W Hilbers

R Van Charldorp

E van Leerdam

P H. Van Knippenberg

L Bosch

Affiliations

Soon will be listed here.

Abstract

The 3' terminus of 16S rRNA has been implicated in the recognition of mRNA's by the ribosome. A fragment containing the 3'-terminal 49 nucleotides cleaved from the rRNA by cloacin DF13 was isolated in a pure form. The secondary structure of this fragment has been studied by measuring the high-resolution proton magnetic resonance spectra. The resonances observed at low field can be assigned to hydrogen-bonded iminoprotons of base-pairs present in the fragment. From the data we conclude that the rRNA fragment, under the conditions used, exists as a hairpin consisting of eight intramolecular base-pairs, the 3'-terminal dodecanucleotide being unpaired. The implications of these findings with respect to the function of the ribosomal protein S1 are discussed.

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