Structural basis of nucleic acid binding by Nicotiana tabacum glycine-rich RNA-binding protein: implications for its RNA chaperone function.
Bottom Line: A HADDOCK model of the NtRRM-RNA complex, based on NMR chemical shift and NOE data, shows that nucleic acid binding results from a combination of stacking and electrostatic interactions with conserved RRM residues.Finally, DNA melting experiments demonstrate that NtGR-RBP1 is more efficient in melting CTG containing nucleic acids than isolated NtRRM.Together, our study supports the model that self-association of GR-RBPs by the glycine-rich region results in cooperative unfolding of non-native substrate structures, thereby enhancing its chaperone function.
Affiliation: NMR Spectroscopy Research Group, Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands Department of Biochemistry, PMAS Agriculture University Rawalpindi, 46300 Rawalpindi, Pakistan.Show MeSH
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Mentions: Tobacco NtGR-RBP1 is a ∼16 kDa protein comprised of an NtRRM domain (85 residues) followed by a glycine-rich region of roughly the same length. Sequence alignment shows that NtGR-RBP1 is highly conserved with orthologous in Arabidopsis and Zea mays sharing 76% and 73% amino acid identity, respectively, and ∼40% homology to mouse, human and bacterial counterparts (Figure 1). Sequence conservation is highest in the NtRRM domain which features the two canonical RNP motifs that have been shown to be required for RNA binding in other RRM domains (2).
Affiliation: NMR Spectroscopy Research Group, Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands Department of Biochemistry, PMAS Agriculture University Rawalpindi, 46300 Rawalpindi, Pakistan.