Charge Influences Substrate Recognition and Self-Assembly of Hydrophobic FG Sequences
Name
090159.full.pdf
Description
Submitted version
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790.51 KB
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Checksum (MD5)
c4a8a80fd39e38965e60679abf493180
Author(s)
Chen, Wesley George
Witten, Jacob Julian Seid
Grindy, Scott Charles
Holten-Andersen, Niels
Ribbeck, Katharina
Date Issued
2017
Journal
Biophysical Journal
Publisher
Elsevier BV
Version
Original manuscript
Abstract
© 2017 Biophysical Society The nuclear pore complex controls the passage of molecules via hydrophobic phenylalanine-glycine (FG) domains on nucleoporins. Such FG domains consist of repeating units of FxFG, FG, or GLFG sequences, many of which are interspersed with highly charged amino acid sequences. Despite the high density of charge in certain FG domains, if and how charge influences FG-domain self-assembly and selective binding of nuclear transport receptors is largely unexplored. Using rationally designed short peptide sequences, we determined that the charge type and identity of amino acids surrounding FG sequences impact the structure and selectivity of FG-based gels. Moreover, we showed that spatial localization of the charged amino acids with respect to the FG sequence determines the degree to which charge influences hydrophobic interactions. Taken together, our study highlights that charge type and placement of amino acids regulate FG-sequence function and are important considerations when studying the mechanism of nuclear pore complex transport in vivo.
MIT Department
Massachusetts Institute of Technology. Department of Biological Engineering
Massachusetts Institute of Technology. Computational and Systems Biology Program
Massachusetts Institute of Technology. Department of Materials Science and Engineering
Terms of Use
Creative Commons Attribution-NonCommercial-NoDerivs License
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DOI of Published Version
https://doi.org/10.1016/J.BPJ.2017.08.058
