High-resolution proton magnetic resonance study of the secondary structure of the 3'-terminal 49-nucleotide fragment of 16S rRNA from Escherichia coli.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 74 ·No. 3 ·1977-03-00 ·Pages 1028-31

Baan RA, Hilbers CW, Van Charldorp R, Van Leerdam E, Van Knippenberg PH, Bosch L

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.

MeSH Terms

Escherichia coli Hydrogen Bonding Magnetic Resonance Spectroscopy Nucleic Acid Conformation RNA, Ribosomal

Chemicals

RNA, Ribosomal

Authors & Affiliations

6 authors, click to expand affiliations / ORCID

Baan R A

Hilbers C W

Van Charldorp R

Van Leerdam E

Van Knippenberg P H

Bosch L

References (17)

17 references, click to expand

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Article Info

Journal

Proceedings of the National Academy of Sciences of the United States of America

Abbr.

Proc Natl Acad Sci U S A

ISSN

0027-8424

DOI

10.1073/pnas.74.3.1028

Published

1977-03-00

Pages

1028-31

Language

English

Region

United States

NLM ID

7505876

PMCID

PMC430575

Subset

External Links

PubMed source DOI: 10.1073/pnas.74.3.1028 PMC Full Text View journal details

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High-resolution proton magnetic resonance study of the secondary structure of the 3'-terminal 49-nucleotide fragment of 16S rRNA from Escherichia coli.

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