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.

journal_name

Nat Struct Mol Biol

authors

Phan AT,Kuryavyi V,Darnell JC,Serganov A,Majumdar A,Ilin S,Raslin T,Polonskaia A,Chen C,Clain D,Darnell RB,Patel DJ

doi

10.1038/nsmb.2064

subject

Has Abstract

pub_date

2011-06-05 00:00:00

pages

796-804

issue

7

eissn

1545-9993

issn

1545-9985

pii

nsmb.2064

journal_volume

18

pub_type

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