BC1-FMRP interaction is modulated by 2'-O-methylation: RNA-binding activity of the tudor domain and translational regulation at synapses.

Details

Serval ID
serval:BIB_1D9179358E45
Type
Article: article from journal or magazin.
Collection
Publications
Title
BC1-FMRP interaction is modulated by 2'-O-methylation: RNA-binding activity of the tudor domain and translational regulation at synapses.
Journal
Nucleic acids research
Author(s)
Lacoux C., Di Marino D., Boyl P.P., Zalfa F., Yan B., Ciotti M.T., Falconi M., Urlaub H., Achsel T., Mougin A., Caizergues-Ferrer M., Bagni C.
ISSN
1362-4962 (Electronic)
ISSN-L
0305-1048
Publication state
Published
Issued date
05/2012
Volume
40
Number
9
Pages
4086-4096
Language
english
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Abstract
The brain cytoplasmic RNA, BC1, is a small non-coding RNA that is found in different RNP particles, some of which are involved in translational control. One component of BC1-containing RNP complexes is the fragile X mental retardation protein (FMRP) that is implicated in translational repression. Peptide mapping and computational simulations show that the tudor domain of FMRP makes specific contacts to BC1 RNA. Endogenous BC1 RNA is 2'-O-methylated in nucleotides that contact the FMRP interface, and methylation can affect this interaction. In the cell body BC1 2'-O-methylations are present in both the nucleus and the cytoplasm, but they are virtually absent at synapses where the FMRP-BC1-mRNA complex exerts its function. These results strongly suggest that subcellular region-specific modifications of BC1 affect the binding to FMRP and the interaction with its mRNA targets. We finally show that BC1 RNA has an important role in translation of certain mRNAs associated to FMRP. All together these findings provide further insights into the translational regulation by the FMRP-BC1 complex at synapses.

Keywords
Animals, Fragile X Mental Retardation Protein/chemistry, Fragile X Mental Retardation Protein/metabolism, Gene Expression Regulation, Methylation, Mice, Mice, Inbred C57BL, Mice, Knockout, Models, Molecular, Neurons/metabolism, Protein Binding, Protein Biosynthesis, Protein Structure, Tertiary, RNA, Messenger/metabolism, RNA, Small Cytoplasmic/chemistry, RNA, Small Cytoplasmic/genetics, RNA, Small Cytoplasmic/metabolism, Synapses/metabolism
Pubmed
Open Access
Yes
Create date
06/03/2017 17:23
Last modification date
20/08/2019 12:53
Usage data