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

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 mi

SUBMITTER: Minde DP 

PROVIDER: S-EPMC6976632 | biostudies-literature | 2020 Jan

REPOSITORIES: biostudies-literature