The Leishmania PABP1–eIF4E4 interface: a novel 5′–3′ interaction architecture for trans-spliced mRNAs

@inproceedings{Rodrigues2019TheLP,
  title={The Leishmania PABP1–eIF4E4 interface: a novel 5′–3′ interaction architecture for trans-spliced mRNAs},
  author={Fabio Henrique dos Santos Rodrigues and Helena Firczuk and Alexander Louis Breeze and Alexander D Cameron and Martin Walko and Andrew J Wilson and Nilson Ivo Tonin Zanchin and John E. G. McCarthy},
  booktitle={Nucleic acids research},
  year={2019}
}
Trans-splicing of trypanosomatid polycistronic transcripts produces polyadenylated monocistronic mRNAs modified to form the 5' cap4 structure (m7Gpppm36,6,2'Apm2'Apm2'Cpm23,2'U). NMR and X-ray crystallography reveal that Leishmania has a unique type of N-terminally-extended cap-binding protein (eIF4E4) that binds via a PAM2 motif to PABP1. This relies on the interactions of a combination of polar and charged amino acid side-chains together with multiple hydrophobic interactions, and underpins a… CONTINUE READING
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