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Data associated with 'Conformational flexibility within the nascent polypeptide–associated complex enables its interactions with structurally diverse client proteins'
Citation
Martin, Esther M. and Jackson, Matthew P. and Gamerdinger, Martin and Gense, Karina and Karamanos, Theodoros and Humes, Julia R. and Deuerling, Elke and Ashcroft, Alison E. and Radford, Sheena E. (2018) Data associated with 'Conformational flexibility within the nascent polypeptide–associated complex enables its interactions with structurally diverse client proteins'. University of Leeds. [Dataset] https://doi.org/10.5518/295
Dataset description
As newly synthesized polypeptides emerge from the ribosome, it is crucial that they fold correctly. To prevent premature aggregation, nascent chains interact with chaperones that facilitate folding or prevent misfolding until protein synthesis is complete. Nascent polypeptide– associated complex (NAC) is a ribosome- associated chaperone important for protein homeostasis. However, how NAC binds its substrates remains unclear. Using native electrospray ionization MS (ESI MS), limited proteolysis, NMR and cross-linking, we analysed the conformational properties of NAC from Caenorhabditis elegans and studied its ability to bind proteins in different conformational states. Our results revealed that NAC adopts an array of compact and expanded conformations and binds weakly to client proteins that are unfolded, folded, or intrinsically disordered, suggestive of broad substrate compatibility. Of note, we found that this weak binding retards aggregation of the intrinsically disordered protein α-synuclein both in vitro and in vivo. These findings provide critical insights into the structure and function of NAC. Specifically, they reveal the ability of NAC to exploit its conformational plasticity to bind a repertoire of substrates having unrelated sequences and structures independently of actively translating ribosomes
| Additional information: | Data uploaded Dec 2017. Paper published April 2018. Changes made 23/07/2018 during the peer review process: Gense added as dataset author and author order revised. Title change from Data associated with 'Structure and function of the nascent polypeptide associated complex revealed by mass spectrometry' to Data associated with 'Conformational flexibility within the nascent polypeptide–associated complex enables its interactions with structurally diverse client proteins'. Abstract updated. | ||||||
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| Keywords: | NAC, native mass spectrometry, NMR, chemical cross-linking | ||||||
| Divisions: | Faculty of Biological Sciences > Astbury Centre for Structural Molecular Biology | ||||||
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| License: | Creative Commons Attribution 4.0 International (CC BY 4.0) | ||||||
| Date deposited: | 14 Dec 2017 21:05 | ||||||
| URI: | https://archive.researchdata.leeds.ac.uk/id/eprint/291 | ||||||
Files
Documentation
Raw data extended file information [13kB]  |
Raw data extended file information [13kB] 
Raw data extended file information [13kB] Data
Peaks Project Data 1 [2GB] |
Peaks Project Data 2 [4GB] |
Peaks Project Data 3 [3GB] |
Raw data - aSynuclein cross-linking [4GB] |
Raw data - Collision induced dissociation data [18MB] |
Raw data - Im7 cross linking data [5GB] |
Raw data - Limited proteolysis [177MB] |
Raw data - NAC BS3 cross-linking [13MB] |
Raw data - Native mass spec data [64MB] |