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Hidden specificity in an apparently nonspecific RNA-binding protein

Author

Listed:
  • Ulf-Peter Guenther

    (Center for RNA Molecular Biology, Case Western Reserve University
    School of Medicine, Case Western Reserve University)

  • Lindsay E. Yandek

    (School of Medicine, Case Western Reserve University)

  • Courtney N. Niland

    (School of Medicine, Case Western Reserve University)

  • Frank E. Campbell

    (Center for RNA Molecular Biology, Case Western Reserve University)

  • David Anderson

    (Zicklin School of Business, Baruch College, The City University of New York)

  • Vernon E. Anderson

    (School of Medicine, Case Western Reserve University)

  • Michael E. Harris

    (School of Medicine, Case Western Reserve University)

  • Eckhard Jankowsky

    (Center for RNA Molecular Biology, Case Western Reserve University
    School of Medicine, Case Western Reserve University)

Abstract

A novel high-throughput sequencing kinetics approach is used to measure functional binding of the apparently nonspecific RNA-binding protein C5 to all possible sequence variants in its substrate binding site; C5 binds different substrate variants with affinities varying widely, and with a similar affinity distribution to that of highly specific nucleic-acid-binding proteins, but it does not bind its physiological RNA targets with the highest affinity.

Suggested Citation

  • Ulf-Peter Guenther & Lindsay E. Yandek & Courtney N. Niland & Frank E. Campbell & David Anderson & Vernon E. Anderson & Michael E. Harris & Eckhard Jankowsky, 2013. "Hidden specificity in an apparently nonspecific RNA-binding protein," Nature, Nature, vol. 502(7471), pages 385-388, October.
    • Handle: RePEc:nat:nature:v:502:y:2013:i:7471:d:10.1038_nature12543
    DOI: 10.1038/nature12543
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