Hidden specificity in an apparently nonspecific RNA-binding protein

Ulf-Peter Guenther, Lindsay E. Yandek, Courtney N. Niland, Frank E. Campbell, David Anderson, Vernon E. Anderson, Michael E. Harris () and Eckhard Jankowsky ()
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Ulf-Peter Guenther: Center for RNA Molecular Biology, 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

Nature, 2013, vol. 502, issue 7471, 385-388

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.

Date: 2013
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DOI: 10.1038/nature12543

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