Use of a semisynthetic epitope to probe histidine kinase activity and regulation

• Published in: Analytical biochemistry Vol. 397; no. 2; pp. 139 - 143
• Main Authors: Carlson, Hans K., Plate, Lars, Price, Mark S., Allen, Jasmina J., Shokat, Kevan M., Marletta, Michael A.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 15.02.2010
• Subjects: Adenosine Triphosphate - analogs & derivatives; Adenosine Triphosphate - metabolism; ATPγS; Cloning, Molecular; Epitopes - chemistry; Escherichia coli - enzymology; Histidine - analogs & derivatives; Histidine - analysis; Histidine - immunology; Histidine Kinase; para-Nitrobenzylmesylate; Protein Kinases - analysis; Protein Kinases - metabolism; Semisynthetic epitope; Thiophosphate; Thiophosphoaspartic acid; Thiophosphohistidine; Thiophosphate; para-Nitrobenzylmesylate; Thiophosphohistidine; Thiophosphoaspartic acid; ATPγS; Histidine kinase; Semisynthetic epitope

Histidine–aspartic acid phosphotransfer pathways are central components of prokaryotic signal transduction pathways and are also found in many eukaryotes. Tools to study histidine kinases, however, are currently quite limited. In this article, we present a new tool to study histidine–aspartic acid p...