Reagent for the detection of protein thiocarboxylates in the bacterial proteome: lissamine rhodamine B sulfonyl azide.
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.
Krishnamoorthy
Kalyanaraman
K
Department of Chemistry, Texas A&M University, College Station, Texas 77840, USA.
Begley
Tadhg P
TP
D001386:Azides / Q000737:chemistry*; D001426:Bacterial Proteins / Q000737:chemistry*; D002264:Carboxylic Acids / Q000737:chemistry*; D007202:Indicators and Reagents / Q000737:chemistry; D015394:Molecular Structure; D020543:Proteome; D044223:Pseudomonas stutzeri / Q000737:chemistry*; D012235:Rhodamines / Q000737:chemistry*; D013237:Stereoisomerism
D001386:Azides; D001426:Bacterial Proteins; D002264:Carboxylic Acids; D007202:Indicators and Reagents; D020543:Proteome; D012235:Rhodamines