Chemical and structural probing of the N-terminal residues encoded by FMR1 exon 15 and their effect on downstream arginine methylation.

@article{Dolzhanskaya2008ChemicalAS,
  title={Chemical and structural probing of the N-terminal residues encoded by FMR1 exon 15 and their effect on downstream arginine methylation.},
  author={Natalia Dolzhanskaya and David Chas Bolton and Robert B. Denman},
  journal={Biochemistry},
  year={2008},
  volume={47 33},
  pages={8491-503}
}
Exon 15 of the fragile X mental retardation protein gene (FMR1) is alternatively spliced into three variants. The amino acids encoded by the 5' end of the exon contain several regulatory determinants including phosphorylation sites and a potential conformational switch. Residues encoded by the 3' end of the exon specify FMRP's RGG box, an RNA binding domain that interacts with G-quartet motifs. Previous studies demonstrated that the exon 15-encoded N-terminal residues influence the extent of… CONTINUE READING