Dataset Information

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

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Dataset's files

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			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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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]

PMID: 31969649

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