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Title: Intrinsically Disordered Protein Exhibits Both Compaction and Expansion under Macromolecular Crowding

Abstract

Conformational malleability allows intrinsically disordered proteins (IDPs) to respond agilely to their environments, such as nonspecifically interacting with in vivo bystander macromolecules (or crowders). Previous studies have emphasized conformational compaction of IDPs due to steric repulsion by macromolecular crowders, but effects of soft attraction are largely unexplored. Here we studied the conformational ensembles of the IDP FlgM in both polymer and protein crowders by small-angle neutron scattering. As crowder concentrations increased, the mean radius of gyration of FlgM first decreased but then exhibited an uptick. Ensemble optimization modeling indicated that FlgM conformations under protein crowding segregated into two distinct populations, one compacted and one extended. Coarse-grained simulations showed that compacted conformers fit into an interstitial void and occasionally bind to a surrounding crowder, whereas extended conformers snake through interstitial crevices and bind multiple crowders simultaneously. In conclusion, crowder-induced conformational segregation may facilitate various cellular functions of IDPs.

Authors:
 [1];  [1]; ORCiD logo [2]; ORCiD logo [2];  [3]
  1. Florida State Univ., Tallahassee, FL (United States)
  2. Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
  3. Florida State Univ., Tallahassee, FL (United States); Univ. of Illinois at Chicago, Chicago, IL (United States)
Publication Date:
Research Org.:
Oak Ridge National Lab. (ORNL), Oak Ridge, TN (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
1479778
Alternate Identifier(s):
OSTI ID: 1495258
Grant/Contract Number:  
AC05-00OR22725
Resource Type:
Journal Article: Accepted Manuscript
Journal Name:
Biophysical Journal
Additional Journal Information:
Journal Volume: 114; Journal Issue: 5; Journal ID: ISSN 0006-3495
Publisher:
Elsevier
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES

Citation Formats

Banks, Anthony, Qin, Sanbo, Weiss, Kevin L., Stanley, Christopher B., and Zhou, Huan -Xiang. Intrinsically Disordered Protein Exhibits Both Compaction and Expansion under Macromolecular Crowding. United States: N. p., 2018. Web. doi:10.1016/j.bpj.2018.01.011.
Banks, Anthony, Qin, Sanbo, Weiss, Kevin L., Stanley, Christopher B., & Zhou, Huan -Xiang. Intrinsically Disordered Protein Exhibits Both Compaction and Expansion under Macromolecular Crowding. United States. doi:10.1016/j.bpj.2018.01.011.
Banks, Anthony, Qin, Sanbo, Weiss, Kevin L., Stanley, Christopher B., and Zhou, Huan -Xiang. Tue . "Intrinsically Disordered Protein Exhibits Both Compaction and Expansion under Macromolecular Crowding". United States. doi:10.1016/j.bpj.2018.01.011. https://www.osti.gov/servlets/purl/1479778.
@article{osti_1479778,
title = {Intrinsically Disordered Protein Exhibits Both Compaction and Expansion under Macromolecular Crowding},
author = {Banks, Anthony and Qin, Sanbo and Weiss, Kevin L. and Stanley, Christopher B. and Zhou, Huan -Xiang},
abstractNote = {Conformational malleability allows intrinsically disordered proteins (IDPs) to respond agilely to their environments, such as nonspecifically interacting with in vivo bystander macromolecules (or crowders). Previous studies have emphasized conformational compaction of IDPs due to steric repulsion by macromolecular crowders, but effects of soft attraction are largely unexplored. Here we studied the conformational ensembles of the IDP FlgM in both polymer and protein crowders by small-angle neutron scattering. As crowder concentrations increased, the mean radius of gyration of FlgM first decreased but then exhibited an uptick. Ensemble optimization modeling indicated that FlgM conformations under protein crowding segregated into two distinct populations, one compacted and one extended. Coarse-grained simulations showed that compacted conformers fit into an interstitial void and occasionally bind to a surrounding crowder, whereas extended conformers snake through interstitial crevices and bind multiple crowders simultaneously. In conclusion, crowder-induced conformational segregation may facilitate various cellular functions of IDPs.},
doi = {10.1016/j.bpj.2018.01.011},
journal = {Biophysical Journal},
issn = {0006-3495},
number = 5,
volume = 114,
place = {United States},
year = {2018},
month = {3}
}

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