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Crystallographic studies of RNA hairpins in complexes with recombinant MS2 capsids: Implications for binding requirements

Published online by Cambridge University Press:  01 January 1999

ELIN GRAHN ,
NICOLA J. STONEHOUSE ,
JAMES B. MURRAY ,
SJOERD VAN DEN WORM ,
KARIN VALEGÅRD ,
KERSTIN FRIDBORG ,
PETER G. STOCKLEY  and
LARS LILJAS
ELIN GRAHN
Affiliation:
Department of Molecular Biology, Uppsala University, Box 590, SE-75124 Uppsala, Sweden
NICOLA J. STONEHOUSE
Affiliation:
School of Biology, University of Leeds, Leeds LS29JT, United Kingdom
JAMES B. MURRAY
Affiliation:
School of Biology, University of Leeds, Leeds LS29JT, United Kingdom Present address: Department of Chemistry, Indiana University, Bloomington, Indiana 47405, USA.
SJOERD VAN DEN WORM
Affiliation:
Department of Molecular Biology, Uppsala University, Box 590, SE-75124 Uppsala, Sweden Present address: Leiden Institute of Chemistry, Gorlaeus Laboratories, Leiden University, PO Box 9502, NL-2300 RA Leiden, The Netherlands.
KARIN VALEGÅRD
Affiliation:
Department of Molecular Biology, Uppsala University, Box 590, SE-75124 Uppsala, Sweden Present address: Department of Biochemistry, Uppsala University, Box 576, SE-75123 Uppsala, Sweden.
KERSTIN FRIDBORG
Affiliation:
Department of Molecular Biology, Uppsala University, Box 590, SE-75124 Uppsala, Sweden
PETER G. STOCKLEY
Affiliation:
School of Biology, University of Leeds, Leeds LS29JT, United Kingdom
LARS LILJAS
Affiliation:
Department of Molecular Biology, Uppsala University, Box 590, SE-75124 Uppsala, Sweden
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Abstract

The coat protein of bacteriophage MS2 is known to bind specifically to an RNA hairpin formed within the MS2 genome. Structurally this hairpin is built up by an RNA double helix interrupted by one unpaired nucleotide and closed by a four-nucleotide loop. We have performed crystallographic studies of complexes between MS2 coat protein capsids and four RNA hairpin variants in order to evaluate the minimal requirements for tight binding to the coat protein and to obtain more information about the three-dimensional structure of these hairpins. An RNA fragment including the four loop nucleotides and a two-base-pair stem but without the unpaired nucleotide is sufficient for binding to the coat protein shell under the conditions used in this study. In contrast, an RNA fragment containing a stem with the unpaired nucleotide but missing the loop nucleotides does not bind to the protein shell.

Keywords

bacteriophage MS2crystal structureRNA bindingRNA–protein interactions
Type
Research Article
Information
RNA , Volume 5 , Issue 1 , January 1999 , pp. 131 - 138
Copyright
© 1999 RNA Society

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