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Protein histidine phosphorylation: Increased stability of thiophosphohistidine

Published online by Cambridge University Press:  01 October 1999

MICHAEL LASKER ,
CUONG D. BUI ,
PAUL G. BESANT ,
KIYOSHI SUGAWARA ,
PHILIP THAI ,
GERGELY MEDZIHRADSZKY  and
CHRISTOPH W. TURCK
MICHAEL LASKER
Affiliation:
Howard Hughes Medical Institute, University of California San Francisco, San Francisco, California 94143-0724
CUONG D. BUI
Affiliation:
Howard Hughes Medical Institute, University of California San Francisco, San Francisco, California 94143-0724
PAUL G. BESANT
Affiliation:
Department of Medicine, University of California San Francisco, San Francisco, California 94143-0724
KIYOSHI SUGAWARA
Affiliation:
Department of Medicine, University of California San Francisco, San Francisco, California 94143-0724
PHILIP THAI
Affiliation:
Department of Medicine, University of California San Francisco, San Francisco, California 94143-0724
GERGELY MEDZIHRADSZKY
Affiliation:
Department of Medicine, University of California San Francisco, San Francisco, California 94143-0724
CHRISTOPH W. TURCK
Affiliation:
Howard Hughes Medical Institute, University of California San Francisco, San Francisco, California 94143-0724 Department of Medicine, University of California San Francisco, San Francisco, California 94143-0724 Cardiovascular Research Institute, University of California San Francisco, San Francisco, California 94143-0724
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Abstract

Posttranslational phosphorylation of proteins is an important event in many cellular processes. Whereas phosphoesters of serine, threonine and tyrosine have been extensively studied, only limited information is available for other amino acids modified by a phosphate group. The formation of phosphohistidine residues in proteins has been discovered in prokaryotic organisms as well as in eukaryotic cells. The ability to biochemically analyze phosphohistidine residues in proteins, however, is severely hampered by its extreme lability under acidic conditions. In our studies we have found that by replacing the phosphate linked to the histidine residue with a thiophosphate, a phosphohistidine derivative with increased stability is formed. This allows the analysis of phosphohistidine-containing proteins by established biochemical techniques and will greatly aid in the investigation of the role of this posttranslational modification in cellular processes.

Keywords

histidine phosphorylationposttranslational modificationsignal transductionthiophosphate
Type
Research Article
Information
Protein Science , Volume 8 , Issue 10 , October 1999 , pp. 2177 - 2185
Copyright
© 1999 The Protein Society

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