PXD016422

PXD016422 is an original dataset announced via ProteomeXchange.

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

Revision	Datetime	Status	ChangeLog Entry
0	2019-11-25 01:41:40	ID requested
⏵ 1	2020-01-29 06:04:30	announced

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]

submitter keyword: Biotin, IDR, E. coli, H. sapiens, LC-SPS-MS3

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

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PRIDE project URI

• PRIDE
  1. PXD016422
     1. Label: PRIDE project
     2. Name: Biotin proximity tagging favors unfolded proteins and enables the study of intrinsically disordered regions