Chemical proteomics with sulfonyl fluoride probes reveals selective labeling of functional tyrosines in glutathione transferases.

Chemical probes have great potential for identifying functional residues in proteins in crude proteomes. Here we studied labeling sites of chemical probes based on sulfonyl fluorides (SFs) on plant and animal proteomes. Besides serine proteases and many other proteins, SF-based probes label Tyr resi...

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Main Authors: Gu, C, Shannon, D, Colby, T, Wang, Z, Shabab, M, Kumari, S, Villamor, J, McLaughlin, C, Weerapana, E, Kaiser, M, Cravatt, B, van der Hoorn, R
Format: Journal article
Language:English
Published: 2013
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author Gu, C
Shannon, D
Colby, T
Wang, Z
Shabab, M
Kumari, S
Villamor, J
McLaughlin, C
Weerapana, E
Kaiser, M
Cravatt, B
van der Hoorn, R
author_facet Gu, C
Shannon, D
Colby, T
Wang, Z
Shabab, M
Kumari, S
Villamor, J
McLaughlin, C
Weerapana, E
Kaiser, M
Cravatt, B
van der Hoorn, R
author_sort Gu, C
collection OXFORD
description Chemical probes have great potential for identifying functional residues in proteins in crude proteomes. Here we studied labeling sites of chemical probes based on sulfonyl fluorides (SFs) on plant and animal proteomes. Besides serine proteases and many other proteins, SF-based probes label Tyr residues in glutathione transferases (GSTs). The labeled GSTs represent four different GST classes that share less than 30% sequence identity. The targeted Tyr residues are located at similar positions in the promiscuous substrate binding site and are essential for GST function. The high selectivity of SF-based probes for functional Tyr residues in GSTs illustrates how these probes can be used for functional studies of GSTs and other proteins in crude proteomes.
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spelling oxford-uuid:107c6b79-8fef-4ee9-a2ce-8e45c4b624942022-03-26T09:56:44ZChemical proteomics with sulfonyl fluoride probes reveals selective labeling of functional tyrosines in glutathione transferases.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:107c6b79-8fef-4ee9-a2ce-8e45c4b62494EnglishSymplectic Elements at Oxford2013Gu, CShannon, DColby, TWang, ZShabab, MKumari, SVillamor, JMcLaughlin, CWeerapana, EKaiser, MCravatt, Bvan der Hoorn, RChemical probes have great potential for identifying functional residues in proteins in crude proteomes. Here we studied labeling sites of chemical probes based on sulfonyl fluorides (SFs) on plant and animal proteomes. Besides serine proteases and many other proteins, SF-based probes label Tyr residues in glutathione transferases (GSTs). The labeled GSTs represent four different GST classes that share less than 30% sequence identity. The targeted Tyr residues are located at similar positions in the promiscuous substrate binding site and are essential for GST function. The high selectivity of SF-based probes for functional Tyr residues in GSTs illustrates how these probes can be used for functional studies of GSTs and other proteins in crude proteomes.
spellingShingle Gu, C
Shannon, D
Colby, T
Wang, Z
Shabab, M
Kumari, S
Villamor, J
McLaughlin, C
Weerapana, E
Kaiser, M
Cravatt, B
van der Hoorn, R
Chemical proteomics with sulfonyl fluoride probes reveals selective labeling of functional tyrosines in glutathione transferases.
title Chemical proteomics with sulfonyl fluoride probes reveals selective labeling of functional tyrosines in glutathione transferases.
title_full Chemical proteomics with sulfonyl fluoride probes reveals selective labeling of functional tyrosines in glutathione transferases.
title_fullStr Chemical proteomics with sulfonyl fluoride probes reveals selective labeling of functional tyrosines in glutathione transferases.
title_full_unstemmed Chemical proteomics with sulfonyl fluoride probes reveals selective labeling of functional tyrosines in glutathione transferases.
title_short Chemical proteomics with sulfonyl fluoride probes reveals selective labeling of functional tyrosines in glutathione transferases.
title_sort chemical proteomics with sulfonyl fluoride probes reveals selective labeling of functional tyrosines in glutathione transferases
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