PXD016422 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Biotin proximity tagging favors unfolded proteins and enables the study of intrinsically disordered regions |
Description | Intrinsically Disordered Regions (IDRs) are enriched in disease-linked proteins known to have multiple post-translational modifications, but there is limited in vivo information about how locally unfolded protein regions contribute to biological functions. We reasoned that IDRs should be more accessible to targeted in vivo biotinylation than ordered protein regions, if they retain their flexibility in vivo. Indeed, we observed increased biotinylation density in predicted IDRs in several cellular compartments >20 000 biotin sites from four human proximity proteomics studies. We show that in a biotin ‘painting’ time course experiment biotinylation events in Escherichia coli ribosomes progress from unfolded and exposed regions at 10 seconds, to structured and less accessible regions after five minutes. We conclude that biotin proximity tagging favours sites of local disorder in proteins and suggest the possibility of using biotin ‘painting’ as a method to gain unique insights into in vivo condition-dependent subcellular plasticity of proteins. |
HostingRepository | PRIDE |
AnnounceDate | 2020-01-29 |
AnnouncementXML | Submission_2020-01-29_06:04:28.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | David-Paul Minde |
SpeciesList | scientific name: Escherichia coli; NCBI TaxID: 562; |
ModificationList | biotinylated residue |
Instrument | Orbitrap Fusion Lumos |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2019-11-25 01:41:40 | ID requested | |
⏵ 1 | 2020-01-29 06:04:30 | announced | |
Publication List
Minde DP, Ramakrishna M, Lilley KS, Biotin proximity tagging favours unfolded proteins and enables the study of intrinsically disordered regions. Commun Biol, 3(1):38(2020) [pubmed] |
Keyword List
submitter keyword: Biotin, IDR, E. coli, H. sapiens, LC-SPS-MS3 |
Contact List
Prof. Kathryn S. Lilley |
contact affiliation | Prof. Kathryn S. Lilley Cambridge Centre for Proteomics Department of Biochemistry University of Cambridge and Milner Therapeutics Institute +441223760255 www.bio.cam.ac.uk/proteomics/ @lilley_ks @CamCProteomics secretary: secretariat@bioc.cam.ac.uk |
contact email | ksl23@cam.ac.uk |
lab head | |
David-Paul Minde |
contact affiliation | CPC |
contact email | dpm43@cam.ac.uk |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD016422
- Label: PRIDE project
- Name: Biotin proximity tagging favors unfolded proteins and enables the study of intrinsically disordered regions