Repository logo
 

Biotin proximity tagging favours unfolded proteins and enables the study of intrinsically disordered regions

Published version
Peer-reviewed

Change log

Authors

Abstract

Abstract: 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 human cells. Indeed, we observed increased biotinylation density in predicted IDRs in several cellular compartments >20,000 biotin sites from four 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 s, 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.

Description

Keywords

Article, /631/45, /631/80, /631/92, /631/114, /631/535, /101, /101/58, /101/47, /101/1, /82, article

Journal Title

Communications Biology

Conference Name

Journal ISSN

2399-3642

Volume Title

3

Publisher

Nature Publishing Group UK
Sponsorship
Thermo Fisher Scientific (Thermo Fisher Scientific Inc.) (2018 Gold level Thermo Scientific Tandem Mass Tag Research Award)
RCUK | Biotechnology and Biological Sciences Research Council (BBSRC) (BB/N010493/1, BB/N010493/1)