Structure-function studies of FMRP RGG peptide recognition of an RNA duplex-quadruplex junction Journal Article
| Authors: | Phan, A. T.; Kuryavyi, V.; Darnell, J. C.; Serganov, A.; Majumdar, A.; Ilin, S.; Raslin, T.; Polonskaia, A.; Chen, C.; Clain, D.; Darnell, R. B.; Patel, D. J. |
| Article Title: | Structure-function studies of FMRP RGG peptide recognition of an RNA duplex-quadruplex junction |
| Abstract: | We have determined the solution structure of the complex between an arginine-glycine-rich RGG peptide from the human fragile X mental retardation protein (FMRP) and an in vitro-selected guanine-rich (G-rich) sc1 RNA. The bound RNA forms a newly discovered G-quadruplex separated from the flanking duplex stem by a mixed junctional tetrad. The RGG peptide is positioned along the major groove of the RNA duplex, with the G-quadruplex forcing a sharp turn of R 10 GGGGR 15 at the duplex-quadruplex junction. Arg10 and Arg15 form cross-strand specificity-determining intermolecular hydrogen bonds with the major-groove edges of guanines of adjacent Watson-Crick G-C pairs. Filter-binding assays on RNA and peptide mutations identify and validate contributions of peptide-RNA intermolecular contacts and shape complementarity to molecular recognition. These findings on FMRP RGG domain recognition by a combination of G-quadruplex and surrounding RNA sequences have implications for the recognition of other genomic G-rich RNAs. © 2011 Nature America, Inc. All rights reserved. |
| Journal Title: | Nature Structural and Molecular Biology |
| Volume: | 18 |
| Issue: | 7 |
| ISSN: | 1545-9993 |
| Publisher: | Nature Publishing Group |
| Date Published: | 2011-06-05 |
| Start Page: | 796 |
| End Page: | 804 |
| Language: | English |
| DOI: | 10.1038/nsmb.2064 |
| PROVIDER: | scopus |
| PMCID: | PMC3130835 |
| PUBMED: | 21642970 |
| DOI/URL: | |
| Notes: | --- - "Export Date: 17 August 2011" - "CODEN: NSMBC" - "Source: Scopus" |
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