Crowder-directed interactions and conformational dynamics in multistimuli-responsive intrinsically disordered protein

Rajkamal Balu; Nisal Wanasingha; Jitendra P Mata; Agata Rekas; Susan Barrett; Geoff Dumsday; Aaron W Thornton; Anita J Hill; Namita Roy Choudhury; Naba K Dutta

doi:10.1126/sciadv.abq2202

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Crowder-directed interactions and conformational dynamics in multistimuli-responsive intrinsically disordered protein

Journal article

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Crowder-directed interactions and conformational dynamics in multistimuli-responsive intrinsically disordered protein

Rajkamal Balu, Nisal Wanasingha, Jitendra P Mata, Agata Rekas, Susan Barrett, Geoff Dumsday, Aaron W Thornton, Anita J Hill, Namita Roy Choudhury and Naba K Dutta

Science advances, Vol.8(51), pp.1-15

21/12/2022

DOI: https://doi.org/10.1126/sciadv.abq2202

PMID: 36542701

Appears in Recent Faculty of Science and Engineering Publications

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Abstract

Intrinsically Disordered Proteins - chemistry

Macromolecular Substances

Protein Conformation

The consequences of crowding on the dynamic conformational ensembles of intrinsically disordered proteins (IDPs) remain unresolved because of their ultrafast motion. Here, we report crowder-induced interactions and conformational dynamics of a prototypical multistimuli-responsive IDP, Rec1-resilin. The effects of a range of crowders of varying sizes, forms, topologies, and concentrations were examined using spectroscopic, spectrofluorimetric, and contrast-matching small- and ultrasmall-angle neutron scattering investigation. To achieve sufficient neutron contrast against the crowders, deuterium-labeled Rec1-resilin was biosynthesized successfully. Moreover, the ab initio “shape reconstruction” approach was used to obtain three-dimensional models of the conformational assemblies. The IDP revealed crowder-specific systematic extension and compaction with the level of macromolecular crowding. Last, a robust extension-contraction model has been postulated to capture the fundamental phenomena governing the observed behavior of IDPs. The study provides insights and fresh perspectives for understanding the interactions and structural dynamics of IDPs in crowded states.

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Title: Crowder-directed interactions and conformational dynamics in multistimuli-responsive intrinsically disordered protein
Creators: Rajkamal Balu - Chemical and Environmental Engineering, School of Engineering, RMIT University, Melbourne, VIC 3000, Australia
Nisal Wanasingha - Chemical and Environmental Engineering, School of Engineering, RMIT University, Melbourne, VIC 3000, Australia
Jitendra P Mata - ANSTO
Agata Rekas - ANSTO
Susan Barrett - CSIRO Manufacturing
Geoff Dumsday - CSIRO Manufacturing
Aaron W Thornton - CSIRO Manufacturing
Anita J Hill - CSIRO Manufacturing
Namita Roy Choudhury - Chemical and Environmental Engineering, School of Engineering, RMIT University, Melbourne, VIC 3000, Australia
Naba K Dutta - Chemical and Environmental Engineering, School of Engineering, RMIT University, Melbourne, VIC 3000, Australia
Publication Details: Science advances, Vol.8(51), pp.1-15
Publisher: American Association for the Advancement of Science
Identifiers: 991013075223202368
Copyright: Copyright © 2022 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution NonCommercial License 4.0 (CC BY-NC).
Academic Unit: Faculty of Science and Engineering; Science
Language: English
Resource Type: Journal article

Crowder-directed interactions and conformational dynamics in multistimuli-responsive intrinsically disordered protein

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