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Reagent for the detection of protein thiocarboxylates in the bacterial proteome: lissamine rhodamine B sulfonyl azide.

ABSTRACT: Protein thiocarboxylates are involved in the biosynthesis of thiamin, molybdopterin, thioquinolobactin, and cysteine. Sequence analysis suggests that this post-translational modification is widely distributed in bacteria. Here we describe the development of lissamine rhodamine B sulfonyl azide as a sensitive click reagent for the detection of protein thiocarboxylates and describe the use of this reagent to detect PdtH, a putative protein thiocarboxylate involved in the biosynthesis of the pyridine dithiocarboxylic acid siderophore, in the Pseudomonas stutzeri proteome.

SUBMITTER: Krishnamoorthy K

PROVIDER: S-EPMC2927480 | biostudies-literature | 2010 Aug

REPOSITORIES: biostudies-literature

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Reagent for the detection of protein thiocarboxylates in the bacterial proteome: lissamine rhodamine B sulfonyl azide.

Krishnamoorthy Kalyanaraman K Begley Tadhg P TP

Journal of the American Chemical Society 20100801 33

Protein thiocarboxylates are involved in the biosynthesis of thiamin, molybdopterin, thioquinolobactin, and cysteine. Sequence analysis suggests that this post-translational modification is widely distributed in bacteria. Here we describe the development of lissamine rhodamine B sulfonyl azide as a sensitive click reagent for the detection of protein thiocarboxylates and describe the use of this reagent to detect PdtH, a putative protein thiocarboxylate involved in the biosynthesis of the pyridi ...[more]

PMID: 20677756

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