4C7Q

Solution structure of the Nt. GR-RBP1 RRM domain

Summary for 4C7Q

• Entry DOI: 10.2210/pdb4c7q/pdb
• NMR Information: BMRB: 19525
• Descriptor: RNA-BINDING GLYCINE-RICH PROTEIN (1 entity in total)
• Functional Keywords: rna binding protein
• Biological source: NICOTIANA TABACUM (COMMON TOBACCO)
• Total number of polymer chains: 1
• Total formula weight: 9537.51

Authors

Kahn, F.,Boelens, R.,Saqlan, S.M.S.,van Ingen, H. (deposition date: 2013-09-24, release date: 2013-10-02, Last modification date: 2024-06-19)

Primary citation

Khan, F.,Boelens, R.,Naqvi, S.M.S.,Van Ingen, H.
Structural Basis of Nucleic Acid Binding by Nicotiana Tabacum Glycine-Rich RNA Binding Protein: Implications for its RNA Chaperone Function
Nucleic Acids Res., 42:8705-, 2014

PubMed Abstract: Glycine-rich RNA-binding proteins (GR-RBPs) are involved in cold shock response of plants as RNA chaperones facilitating mRNA transport, splicing and translation. GR-RBPs are bipartite proteins containing a RNA recognition motif (RRM) followed by a glycine-rich region. Here, we studied the structural basis of nucleic acid binding of full-length Nicotiana tabacum GR-RBP1. NMR studies of NtGR-RBP1 show that the glycine-rich domain, while intrinsically disordered, is responsible for mediating self-association by transient interactions with its RRM domain (NtRRM). Both NtGR-RBP1 and NtRRM bind specifically and with low micromolar affinity to RNA and single-stranded DNA. The solution structure of NtRRM shows that it is a canonical RRM domain. 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.

PubMed: 24957607
DOI: 10.1093/NAR/GKU468

Experimental method

SOLUTION NMR