PXD035668 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Disordered region encodes α-crystallin chaperone activity toward lens client γD-crystallin |
Description | Small heat-shock proteins (sHSPs) are a widely expressed family of ATP-independent molecular chaperones that are among the first responders to cellular stress. Mechanisms by which sHSPs delay aggregation of client proteins remain undefined. sHSPs have high intrinsic disorder content of up to ~60% and assemble into large, polydisperse homo- and hetero-oligomers, making them challenging structural and biochemical targets. Two sHSPs, HSPB4 and HSPB5, are present at millimolar concentrations in eye lens, where they are responsible for maintaining lens transparency over the lifetime of an organism. Together, HSPB4 and HSPB5 compose the hetero-oligomeric chaperone known as α-crystallin. To identify the determinants of sHSP function, we compared the effectiveness of HSPB4 and HSPB5 homo-oligomers and HSPB4/HSPB5 hetero-oligomers in delaying the aggregation of the lens protein γD-crystallin. In chimeric versions of HSPB4 and HSPB5, chaperone activity tracked with the identity of the 60-residue disordered N-terminal regions (NTR). A short 10-residue stretch in the middle of the NTR (“Critical sequence”) contains three residues that are responsible for high HSPB5 chaperone activity toward γD-crystallin. These residues affect structure and dynamics throughout the NTR. Abundant interactions involving the NTR Critical sequence reveal it to be a hub for a network of interactions within oligomers. We propose a model whereby the NTR critical sequence influences local structure and NTR dynamics that modulate accessibility of the NTR, which in turn modulates chaperone activity. |
HostingRepository | PRIDE |
AnnounceDate | 2023-01-31 |
AnnouncementXML | Submission_2023-01-31_11:02:09.627.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Lindsey D.Ulmer |
SpeciesList | scientific name: Escherichia coli; NCBI TaxID: 562; |
ModificationList | No PTMs are included in the dataset |
Instrument | Orbitrap Fusion Lumos |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2022-08-01 02:40:37 | ID requested | |
⏵ 1 | 2023-01-31 11:02:09 | announced | |
Publication List
Dataset with its publication pending |
Keyword List
submitter keyword: HSPB5,Small Heat Shock Proteins, Crosslinking, BPA |
Contact List
Matthew F.Bush |
contact affiliation | University of Washington Department of Chemistry |
contact email | mattbush@uw.edu |
lab head | |
Lindsey D.Ulmer |
contact affiliation | University of Washington Department of Chemistry |
contact email | lulmer@uw.edu |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD035668
- Label: PRIDE project
- Name: Disordered region encodes α-crystallin chaperone activity toward lens client γD-crystallin