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Kee, Jung-Min
Bioorganic and Chembio Lab
Research Interests
  • Chemical biology, organic synthesis, peptide chemistry, synthetic protein chemistry

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A pan-specific antibody for direct detection of protein histidine phosphorylation

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Title
A pan-specific antibody for direct detection of protein histidine phosphorylation
Author
Kee, Jung-MinOslund, Rob C.Perlman, David H.Muir, Tom W.
Issue Date
2013-07
Publisher
NATURE PUBLISHING GROUP
Citation
NATURE CHEMICAL BIOLOGY, v.9, no.7, pp.416 - 421
Abstract
Despite its importance in central metabolism and bacterial cell signaling, protein histidine phosphorylation has remained elusive with respect to its extent and functional roles in biological systems because of the lack of adequate research tools. We report the development of the first pan-phosphohistidine (pHis) antibody using a stable pHis mimetic as the hapten. This antibody was successfully used in ELISA, western blotting, dot blot assays and immunoprecipitation and in detection and identification of histidine-phosphorylated proteins from native cell lysates when coupled with MS analysis. We also observed that the amount of protein pHis in Escherichia coli lysates depends on carbon source and nitrogen availability in the growth medium. In particular, we found that the amount of pHis on phosphoenolpyruvate synthase (PpsA) is sensitive to nitrogen availability in vivo and that α-ketoglutarate inhibits phosphotransfer from phosphorylated PpsA to pyruvate. We expect this antibody to open opportunities for investigating other pHis proteins and their functions. © 2013 Nature America, Inc.
URI
https://scholarworks.unist.ac.kr/handle/201301/13396
URL
http://www.nature.com/nchembio/journal/v9/n7/full/nchembio.1259.html
DOI
10.1038/NCHEMBIO.1259
ISSN
1552-4450
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CHM_Journal Papers
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