Charge Influences Substrate Recognition and Self-Assembly of Hydrophobic FG Sequences
© 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...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Elsevier BV
2021
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| Online Access: | https://hdl.handle.net/1721.1/134686 |
| _version_ | 1826212391769079808 |
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| author | Chen, Wesley G Witten, Jacob Grindy, Scott C Holten-Andersen, Niels Ribbeck, Katharina |
| author_facet | Chen, Wesley G Witten, Jacob Grindy, Scott C Holten-Andersen, Niels Ribbeck, Katharina |
| author_sort | Chen, Wesley G |
| collection | MIT |
| description | © 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. |
| first_indexed | 2024-09-23T15:20:40Z |
| format | Article |
| id | mit-1721.1/134686 |
| institution | Massachusetts Institute of Technology |
| language | English |
| last_indexed | 2024-09-23T15:20:40Z |
| publishDate | 2021 |
| publisher | Elsevier BV |
| record_format | dspace |
| spelling | mit-1721.1/1346862022-03-29T20:51:32Z Charge Influences Substrate Recognition and Self-Assembly of Hydrophobic FG Sequences Chen, Wesley G Witten, Jacob Grindy, Scott C Holten-Andersen, Niels Ribbeck, Katharina © 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. 2021-10-27T20:06:10Z 2021-10-27T20:06:10Z 2017 2019-09-19T14:59:14Z Article http://purl.org/eprint/type/JournalArticle https://hdl.handle.net/1721.1/134686 en 10.1016/J.BPJ.2017.08.058 Biophysical Journal Creative Commons Attribution-NonCommercial-NoDerivs License http://creativecommons.org/licenses/by-nc-nd/4.0/ application/pdf Elsevier BV bioRxiv |
| spellingShingle | Chen, Wesley G Witten, Jacob Grindy, Scott C Holten-Andersen, Niels Ribbeck, Katharina Charge Influences Substrate Recognition and Self-Assembly of Hydrophobic FG Sequences |
| title | Charge Influences Substrate Recognition and Self-Assembly of Hydrophobic FG Sequences |
| title_full | Charge Influences Substrate Recognition and Self-Assembly of Hydrophobic FG Sequences |
| title_fullStr | Charge Influences Substrate Recognition and Self-Assembly of Hydrophobic FG Sequences |
| title_full_unstemmed | Charge Influences Substrate Recognition and Self-Assembly of Hydrophobic FG Sequences |
| title_short | Charge Influences Substrate Recognition and Self-Assembly of Hydrophobic FG Sequences |
| title_sort | charge influences substrate recognition and self assembly of hydrophobic fg sequences |
| url | https://hdl.handle.net/1721.1/134686 |
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