Proteomics

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Biotin proximity tagging favors 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 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.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Escherichia Coli

SUBMITTER: David-Paul Minde  

LAB HEAD: Prof. Kathryn S. Lilley

PROVIDER: PXD016422 | Pride | 2020-01-29

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
70S_Paint_Kinetics_10_120_300_7200_long.raw Raw
70S_Paint_Kinetics_10_120_300_7200_short.raw Raw
70S_VITRO_KIN_PD23.msf Msf
70S_VITRO_KIN_PD23.pep.xml Pepxml
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Publications

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

Minde David-Paul DP   Ramakrishna Manasa M   Lilley Kathryn S KS  

Communications biology 20200122 1


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 c  ...[more]

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