Sulfonation and phosphorylation of regions of the dioxin receptor susceptible to methionine modifications.

Keyur A Dave, Fiona Whelan, Colleen Bindloss, Sebastian George Furness, Anne Chapman-Smith, Murray L Whitelaw, Jeffrey J Gorman

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Abstract

Tagged murine dioxin receptor was purified from mammalian cells, digested with trypsin, and analyzed by capillary HPLC-MALDI-TOF/TOF-MS and -MS/MS. Several chromatographically distinct semitryptic peptides matching two regions spanning residues Glu(409)-Arg(424) and Ser(547)-Arg(555) of the dioxin receptor were revealed by de novo sequencing. Methionine residues at 418 and 548 were detected in these peptides as either unmodified or modified by moieties of 16 (oxidation) or 57 amu (S-carboxamidomethylation) or in a form corresponding to degradative removal of 105 amu from the S-carboxamidomethylated methionine. MS/MS spectra revealed that the peptides containing modified methionine residues also existed in forms with a modification of +80 amu on serine residues 411, 415, and 547. The MS/MS spectra of these peptide ions also revealed diagnostic neutral loss fragment ions of 64, 98, and/or 80 amu, and in some instances combinations of these neutral losses were apparent.......
Original languageEnglish
Pages (from-to)706 - 719
Number of pages14
JournalMolecular & Cellular Proteomics
Volume8
Issue number4
DOIs
Publication statusPublished - 2009

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