التفاصيل البيبلوغرافية
| العنوان: |
Structural basis of nucleic acid binding by Nicotiana tabacum glycine-rich RNA-binding protein: Implications for its RNA chaperone function |
| المؤلفون: |
Khan, Fariha, Daniëls, Mark A., Folkers, Gert E., Boelens, Rolf, Saqlan Naqvi, S. M., Van Ingen, Hugo |
| المساهمون: |
NMR Spectroscopy, Sub NMR Spectroscopy |
| سنة النشر: |
2014 |
| مصطلحات موضوعية: |
COLD ADAPTATION PROCESS, TORSION ANGLE DYNAMICS, ARABIDOPSIS-THALIANA, MESSENGER-RNA, RECOGNITION MOTIF, NMR-SPECTROSCOPY, CHEMICAL-SHIFTS, PLANT IMMUNITY, FEEDBACK LOOP, III EFFECTOR, Genetics |
| الوصف: |
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. |
| نوع الوثيقة: |
article in journal/newspaper |
| وصف الملف: |
image/pdf |
| اللغة: |
English |
| تدمد: |
0305-1048 |
| العلاقة: |
https://dspace.library.uu.nl/handle/1874/307161Test |
| الإتاحة: |
https://dspace.library.uu.nl/handle/1874/307161Test |
| حقوق: |
info:eu-repo/semantics/OpenAccess |
| رقم الانضمام: |
edsbas.99049944 |
| قاعدة البيانات: |
BASE |
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