A significant number of proteins in both eukaryotes and prokaryotes are known to be post-translationally modified by the addition of phosphate, serving as a means of rapidly regulating protein function. Phosphorylation of the amino acids serine, threonine and tyrosine are the focus of the vast majority of studies aimed at elucidating the extent and roles of such modification, yet other amino acids, including histidine and aspartate, are also phosphorylated. Although histidine phosphorylation is known to play extensive roles in signalling in eukaryotes, plants and fungi, roles for phosphohistidine are poorly defined in higher eukaryotes. Characterization of histidine phosphorylation aimed at elucidating such information is problematic due to the acid-labile nature of the phosphoramidate bond, essential for many of its biological functions. Although MS-based strategies have proven extremely useful in the analysis of other types of phosphorylated peptides, the chromatographic procedures essential for such approaches promote rapid hydrolysis of phosphohistidine-containing peptides. Phosphate transfer to non-biologically relevant aspartate residues during MS analysis further complicates the scenario.
Skip Nav Destination
Article navigation
August 2013
-
Cover Image
Cover Image
- PDF Icon PDF LinkFront Matter
- PDF Icon PDF LinkTable of Contents
Conference Article|
July 18 2013
Attempting to rewrite History: challenges with the analysis of histidine-phosphorylated peptides
Maria-Belen Gonzalez-Sanchez;
Maria-Belen Gonzalez-Sanchez
1
*Michael Barber Centre for Mass Spectrometry, Manchester Institute of Biotechnology, School of Chemistry, University of Manchester, 131 Princess Street, Manchester M1 7DN, U.K.
Search for other works by this author on:
Francesco Lanucara;
Francesco Lanucara
1
*Michael Barber Centre for Mass Spectrometry, Manchester Institute of Biotechnology, School of Chemistry, University of Manchester, 131 Princess Street, Manchester M1 7DN, U.K.
†Protein Function Group, Institute of Integrative Biology, University of Liverpool, Crown Street, Liverpool L69 7ZB, U.K.
Search for other works by this author on:
Matthew Helm;
Matthew Helm
‡School of Chemistry and Chemical Engineering, Queen's University Belfast, Stranmills Road, Belfast BT9 5AG, Northern Ireland, U.K.
Search for other works by this author on:
Claire E. Eyers
Claire E. Eyers
2
*Michael Barber Centre for Mass Spectrometry, Manchester Institute of Biotechnology, School of Chemistry, University of Manchester, 131 Princess Street, Manchester M1 7DN, U.K.
†Protein Function Group, Institute of Integrative Biology, University of Liverpool, Crown Street, Liverpool L69 7ZB, U.K.
2To whom correspondence should be addressed (emailClaire.Eyers@Liverpool.ac.uk).
Search for other works by this author on:
Publisher: Portland Press Ltd
Received:
May 01 2013
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2013 Biochemical Society
2013
Biochem Soc Trans (2013) 41 (4): 1089–1095.
Article history
Received:
May 01 2013
Citation
Maria-Belen Gonzalez-Sanchez, Francesco Lanucara, Matthew Helm, Claire E. Eyers; Attempting to rewrite History: challenges with the analysis of histidine-phosphorylated peptides. Biochem Soc Trans 1 August 2013; 41 (4): 1089–1095. doi: https://doi.org/10.1042/BST20130072
Download citation file:
Sign in
Don't already have an account? Register
Sign in to your personal account
You could not be signed in. Please check your email address / username and password and try again.
Captcha Validation Error. Please try again.