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

Lacoux, C., Di Marino, D., Boyl, P. P., Zalfa, F., Yan, B., Ciotti, M. T., et al. (2012). BC1-FMRP interaction is modulated by 2'-O-methylation: RNA-binding activity of the tudor domain and translational regulation at synapses. Nucleic Acids Research, 40(9), 4086-4096. doi:10.1093/nar/gkr1254.

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 Urheber:
Lacoux, C., Autor
Di Marino, D., Autor
Boyl, P. P., Autor
Zalfa, F., Autor
Yan, B., Autor
Ciotti, M. T., Autor
Falconi, M., Autor
Urlaub, H.1, Autor           
Achsel, T., Autor
Mougin, A., Autor
Caizergues-Ferrer, M., Autor
Baigni, C., Autor
Affiliations:
1Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society, ou_578613              

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 Zusammenfassung: The brain cytoplasmic RNA, BC1 , is a small non-coding RNA that is found in different RNP par- ticles, 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 0 - O -methylated in nucleotides that contact the FMRP interface, and methylation can affect this interaction. In the cell body BC1 2 0 - 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.

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Sprache(n): eng - English
 Datum: 2012-01-112012-05
 Publikationsstatus: Erschienen
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 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1093/nar/gkr1254
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Titel: Nucleic Acids Research
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Seiten: - Band / Heft: 40 (9) Artikelnummer: - Start- / Endseite: 4086 - 4096 Identifikator: -