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Phosphorylated serine and threonine residues promote site-specific fragmentation of singly charged, arginine-containing peptide ions.
Rapid Commun Mass Spectrom. 2009 May; 23(10):1435-45.RC

Abstract

In order to investigate gas-phase fragmentation reactions of phosphorylated peptide ions, matrix-assisted laser desorption/ionization (MALDI) and electrospray ionization (ESI) tandem mass (MS/MS) spectra were recorded from synthetic phosphopeptides and from phosphopeptides isolated from natural sources. MALDI-TOF/TOF (TOF: time-of-flight) spectra of synthetic arginine-containing phosphopeptides revealed a significant increase of y ions resulting from bond cleavages on the C-terminal side of phosphothreonine or phosphoserine. The same effect was found in ESI-MS/MS spectra recorded from the singly charged but not from the doubly charged ions of these phosphopeptides. ESI-MS/MS spectra of doubly charged phosphopeptides containing two arginine residues support the following general fragmentation rule: Increased amide bond cleavage on the C-terminal side of phosphorylated serines or threonines mainly occurs in peptide ions which do not contain mobile protons. In MALDI-TOF/TOF spectra of phosphopeptides displaying N-terminal fragment ions, abundant b-H(3)PO(4) ions resulting from the enhanced dissociation of the pSer/pThr-X bond were detected (X denotes amino acids). Cleavages at phosphoamino acids were found to be particularly predominant in spectra of phosphopeptides containing pSer/pThr-Pro bonds. A quantitative evaluation of a larger set of MALDI-TOF/TOF spectra recorded from phosphopeptides indicated that phosphoserine residues in arginine-containing peptides increase the signal intensities of the respective y ions by almost a factor of 3. A less pronounced cleavage-enhancing effect was observed in some lysine-containing phosphopeptides without arginine. The proposed peptide fragmentation pathways involve a nucleophilic attack by phosphate oxygen on the carbon center of the peptide backbone amide, which eventually leads to cleavage of the amide bond.

Authors+Show Affiliations

Functional Genomics Center Zurich, University of Zurich, Winterthurerstrasse 190, 8057 Zurich, Switzerland. peter.gehrig@fgcz.uzh.chNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

19353557

Citation

Gehrig, Peter Max, et al. "Phosphorylated Serine and Threonine Residues Promote Site-specific Fragmentation of Singly Charged, Arginine-containing Peptide Ions." Rapid Communications in Mass Spectrometry : RCM, vol. 23, no. 10, 2009, pp. 1435-45.
Gehrig PM, Roschitzki B, Rutishauser D, et al. Phosphorylated serine and threonine residues promote site-specific fragmentation of singly charged, arginine-containing peptide ions. Rapid Commun Mass Spectrom. 2009;23(10):1435-45.
Gehrig, P. M., Roschitzki, B., Rutishauser, D., Reiland, S., & Schlapbach, R. (2009). Phosphorylated serine and threonine residues promote site-specific fragmentation of singly charged, arginine-containing peptide ions. Rapid Communications in Mass Spectrometry : RCM, 23(10), 1435-45. https://doi.org/10.1002/rcm.4019
Gehrig PM, et al. Phosphorylated Serine and Threonine Residues Promote Site-specific Fragmentation of Singly Charged, Arginine-containing Peptide Ions. Rapid Commun Mass Spectrom. 2009;23(10):1435-45. PubMed PMID: 19353557.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Phosphorylated serine and threonine residues promote site-specific fragmentation of singly charged, arginine-containing peptide ions. AU - Gehrig,Peter Max, AU - Roschitzki,Bernd, AU - Rutishauser,Dorothea, AU - Reiland,Sonja, AU - Schlapbach,Ralph, PY - 2009/4/9/entrez PY - 2009/4/9/pubmed PY - 2009/9/2/medline SP - 1435 EP - 45 JF - Rapid communications in mass spectrometry : RCM JO - Rapid Commun Mass Spectrom VL - 23 IS - 10 N2 - In order to investigate gas-phase fragmentation reactions of phosphorylated peptide ions, matrix-assisted laser desorption/ionization (MALDI) and electrospray ionization (ESI) tandem mass (MS/MS) spectra were recorded from synthetic phosphopeptides and from phosphopeptides isolated from natural sources. MALDI-TOF/TOF (TOF: time-of-flight) spectra of synthetic arginine-containing phosphopeptides revealed a significant increase of y ions resulting from bond cleavages on the C-terminal side of phosphothreonine or phosphoserine. The same effect was found in ESI-MS/MS spectra recorded from the singly charged but not from the doubly charged ions of these phosphopeptides. ESI-MS/MS spectra of doubly charged phosphopeptides containing two arginine residues support the following general fragmentation rule: Increased amide bond cleavage on the C-terminal side of phosphorylated serines or threonines mainly occurs in peptide ions which do not contain mobile protons. In MALDI-TOF/TOF spectra of phosphopeptides displaying N-terminal fragment ions, abundant b-H(3)PO(4) ions resulting from the enhanced dissociation of the pSer/pThr-X bond were detected (X denotes amino acids). Cleavages at phosphoamino acids were found to be particularly predominant in spectra of phosphopeptides containing pSer/pThr-Pro bonds. A quantitative evaluation of a larger set of MALDI-TOF/TOF spectra recorded from phosphopeptides indicated that phosphoserine residues in arginine-containing peptides increase the signal intensities of the respective y ions by almost a factor of 3. A less pronounced cleavage-enhancing effect was observed in some lysine-containing phosphopeptides without arginine. The proposed peptide fragmentation pathways involve a nucleophilic attack by phosphate oxygen on the carbon center of the peptide backbone amide, which eventually leads to cleavage of the amide bond. SN - 1097-0231 UR - https://www.unboundmedicine.com/medline/citation/19353557/Phosphorylated_serine_and_threonine_residues_promote_site_specific_fragmentation_of_singly_charged_arginine_containing_peptide_ions_ DB - PRIME DP - Unbound Medicine ER -