Oligonucleotide binding specificities of the hnRNP C protein tetramer.

@article{Soltaninassab1998OligonucleotideBS,
  title={Oligonucleotide binding specificities of the hnRNP C protein tetramer.},
  author={Syrus R Soltaninassab and J G McAfee and L Shahied-Milam and Wallace Lestourgeon},
  journal={Nucleic acids research},
  year={1998},
  volume={26 14},
  pages={3410-7}
}
Through the use of various non-equilibrium RNA binding techniques, the C protein tetramer of mammalian40S hnRNP particles has been characterized previously as a poly(U) binding protein with specificity for the pyrimidine-rich sequences that often precede 3' intron-exon junctions. C protein has also been characterized as a sequence-independent RNA chaperonin that is distributed along nascent transcripts through cooperative binding and as a protein ruler that defines the length of RNA packaged in… CONTINUE READING