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      Detecting the Site of Phosphorylation in Phosphopeptides Without Loss of Phosphate Group Using MALDI TOF Mass Spectrometry

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          Abstract

          Phosphopeptides with one and four phosphate groups were characterized by MALDI mass spectrometry. The molecular ion of monophosphopeptide could be detected both as positive and negative ions by MALDI TOF with delayed extraction (DE) and in the reflector mode. The tetraphospho peptide could be detected in linear mode. When MS/MS spectra of the monophospho peptides were obtained in a MALDI TOF TOF instrument by CID, b and y ions with the intact phosphate group were observed, in addition the b and y ions without the phosphate group. Our study indicates that it is possible to detect phosphorylated peptides with out the loss of phosphate group by MALDI TOF as well as MALDI TOF TOF instruments with delayed extraction and in the reflector mode.

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          Two-component signal transduction.

          A M Stock, V L Robinson, P Goudreau (2000)
          Most prokaryotic signal-transduction systems and a few eukaryotic pathways use phosphotransfer schemes involving two conserved components, a histidine protein kinase and a response regulator protein. The histidine protein kinase, which is regulated by environmental stimuli, autophosphorylates at a histidine residue, creating a high-energy phosphoryl group that is subsequently transferred to an aspartate residue in the response regulator protein. Phosphorylation induces a conformational change in the regulatory domain that results in activation of an associated domain that effects the response. The basic scheme is highly adaptable, and numerous variations have provided optimization within specific signaling systems. The domains of two-component proteins are modular and can be integrated into proteins and pathways in a variety of ways, but the core structures and activities are maintained. Thus detailed analyses of a relatively small number of representative proteins provide a foundation for understanding this large family of signaling proteins.
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            State-of-the-art in phosphoproteomics.

            Joerg Reinders, Albert Sickmann (2005)
            Presently, phosphorylation of proteins is the most studied and best understood PTM. However, the analysis of phosphoproteins and phosphopeptides is still one of the most challenging tasks in contemporary proteome research. Since not every phosphoprotein is accessible by a certain method and identification of the phosphorylated amino acid residue is required in the majority of cases, various strategies for the detection and localization of phosphorylations have been developed. Identification and localization of protein phosphorylations is mostly done by MS nowadays but phosphoproteins and -peptides are often suppressed in comparison to the unphosphorylated species if measured in complex mixtures. Thus, the isolation of pure phosphopeptide samples is a main task. This review gives an overview over the most frequently used methods in isolation and detection of phosphoproteins and -peptides such as specific enrichment or separation strategies as well as the localization of the phosphorylated residues by various mass spectrometric techniques.
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              Charging it up: global analysis of protein phosphorylation.

              Jason Ptacek, Michael Snyder (2006)
              Protein phosphorylation affects most, if not all, cellular activities in eukaryotes and is essential for cell proliferation and development. An estimated 30% of cellular proteins are phosphorylated, representing the phosphoproteome, and phosphorylation can alter a protein's function, activity, localization and stability. Recent studies for large-scale identification of phosphosites using mass spectrometry are revealing the components of the phosphoproteome. The development of new tools, such as kinase assays using modified kinases or protein microarrays, enables rapid kinase substrate identification. The dynamics of specific phosphorylation events can now be monitored using mass spectrometry, single-cell analysis of flow cytometry, or fluorescent reporters. Together, these techniques are beginning to elucidate cellular processes and pathways regulated by phosphorylation, in addition to global regulatory networks.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Anal Chem Insights
                Journal ID (publisher-id): Analytical Chemistry Insights
                Title: Analytical Chemistry Insights
                Publisher: Libertas Academica
                ISSN (Electronic): 1177-3901
                Publication date Collection: 2008
                Publication date (Electronic): 26 February 2008
                Volume: 3
                Pages: 21-29
                Affiliations
                Centre for Cellular and Molecular Biology, Uppal Road, Hyderabad 500 007, India
                Author notes
                Correspondence: Dr. M.V. Jagannadham and Dr. R. Nagaraj, Tel: + 91-40-27192589; Fax: + 91-40-27160591; Email: jagan@ 123456ccmb.res.in and nraj@ 123456ccmb.res.in
                Article
                Publisher ID: aci-3-21
                PMC ID: 2701175
                PubMed ID: 19609387
                SO-VID: 0fae7431-bf48-40b0-a312-812f7c8f1cda
                Copyright © Copyright © 2008 The authors.
                License:

                This article is published under the Creative Commons Attribution By licence. For further information go to: http://creativecommons.org/licenses/by/3.0.

                History
                Categories
                Subject: Original Research

                ScienceOpen disciplines: Analytical chemistry
                Keywords: neutral loss,linear mode,positive ion,reflector mode,phosphopeptides,mass spectrometry
                Data availability:
                ScienceOpen disciplines: Analytical chemistry
                Keywords: neutral loss, linear mode, positive ion, reflector mode, phosphopeptides, mass spectrometry

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