RNA-binding proteins

RNA-binding proteins are proteins that bind to ribonucleic acid (RNA) molecules, are generally found in the cytoplasm and nucleus, and are important in forming ribonucleoproteins (RNPs). One type of RNP, hnRNPs (heteronuclear proteins), are important in splicing of mRNA (messenger RNA), polyadenylation, stabilization, localization and translation.

Latest Research and Reviews

  • Research
    | Open Access

    The HIV-1 RNA-binding protein rev facilitates nuclear export of viral RNA. Here, the authors use native mass spectrometry to study the interactions between rev-derived peptides and rev response elements of HIV-1 RNA, providing mechanistic insights into rev recognition and recruitment.

    • Eva-Maria Schneeberger
    • , Matthias Halper
    • , Michael Palasser
    • , Sarah Viola Heel
    • , Jovana Vušurović
    • , Raphael Plangger
    • , Michael Juen
    • , Christoph Kreutz
    •  & Kathrin Breuker
  • Research
    | Open Access

    So far only a few compounds have been reported as splicing modulators. Here, the authors combine high-throughput screening, chemical synthesis, NMR, X-ray crystallography with functional studies and develop phenothiazines as inhibitors for the U2AF Homology Motif (UHM) domains of proteins that regulate splicing and show that they inhibit early spliceosome assembly on pre-mRNA substrates in vitro.

    • Pravin Kumar Ankush Jagtap
    • , Tomáš Kubelka
    • , Komal Soni
    • , Cindy L. Will
    • , Divita Garg
    • , Claudia Sippel
    • , Tobias G. Kapp
    • , Harish Kumar Potukuchi
    • , Kenji Schorpp
    • , Kamyar Hadian
    • , Horst Kessler
    • , Reinhard Lührmann
    • , Felix Hausch
    • , Thorsten Bach
    •  & Michael Sattler
  • Research
    | Open Access

    Human ADAR proteins are responsible for RNA editing, conversion of adenosine to inosine in double-stranded RNA. Here the authors report a previously unknown zinc ion-binding site in the catalytic domain of human ADAR1 using high throughput mutagenesis, biochemical assay and Rosetta-based protein structure modeling.

    • SeHee Park
    • , Erin E. Doherty
    • , Yixuan Xie
    • , Anil K. Padyana
    • , Fang Fang
    • , Yue Zhang
    • , Agya Karki
    • , Carlito B. Lebrilla
    • , Justin B. Siegel
    •  & Peter A. Beal
  • Research |

    A protein condensate formed by multivalent interactions between the long non-coding RNA Xist and specific RNA-binding proteins drives the compartmentalization required to perpetuate gene silencing on the inactive X chromosome.

    • Amy Pandya-Jones
    • , Yolanda Markaki
    • , Jacques Serizay
    • , Tsotne Chitiashvili
    • , Walter R. Mancia Leon
    • , Andrey Damianov
    • , Constantinos Chronis
    • , Bernadett Papp
    • , Chun-Kan Chen
    • , Robin McKee
    • , Xiao-Jun Wang
    • , Anthony Chau
    • , Shan Sabri
    • , Heinrich Leonhardt
    • , Sika Zheng
    • , Mitchell Guttman
    • , Douglas. L. Black
    •  & Kathrin Plath
    Nature 587, 145-151

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