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Jonker HR, Ilin S, Grimm SK, Wöhnert J, Schwalbe H. Nucleic
Acids Res. 2007;35(2):441-54
L11 domain rearrangement upon binding to RNA and
thiostrepton studied by NMR spectroscopy.
Johann Wolfgang Goethe-University, Institute for Organic
Chemistry and Chemical Biology, Center for Biomolecular Magnetic
Resonance, Max-von-Laue-Strasse 7, 60438 Frankfurt am Main,
Germany.
Ribosomal proteins are assumed to stabilize specific RNA
structures and promote compact folding of the large rRNA. The
conformational dynamics of the protein between the bound and
unbound state play an important role in the binding process. We
have studied those dynamical changes in detail for the highly
conserved complex between the ribosomal protein L11 and the
GTPase region of 23S rRNA. The RNA domain is compactly folded
into a well defined tertiary structure, which is further
stabilized by the association with the C-terminal domain of the
L11 protein (L11(ctd)). In addition, the N-terminal domain of
L11 (L11(ntd)) is implicated in the binding of the natural
thiazole antibiotic thiostrepton, which disrupts the elongation
factor function. We have studied the conformation of the
ribosomal protein and its dynamics by NMR in the unbound state,
the RNA bound state and in the ternary complex with the RNA and
thiostrepton. Our data reveal a rearrangement of the L11(ntd),
placing it closer to the RNA after binding of thiostrepton,
which may prevent binding of elongation factors. We propose a
model for the ternary L11-RNA-thiostrepton complex that is
additionally based on interaction data and conformational
information of the L11 protein. The model is consistent with
earlier findings and provides an explanation for the role of
L11(ntd) in elongation factor binding.
PMID: 17169991 |
