Ion-selective enrichment of tyrosine-sulfated peptides from complex protein digests

Amano, Yukari; Shinohara, Hidefumi; Sakagami, Youji; Matsubayashi, Yoshikatsu

doi:10.1016/j.ab.2005.06.047

Cited by 24 publications

(31 citation statements)

References 26 publications

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“…We performed ion-selective enrichment of sulfated peptides by using Arabidopsis T-87 suspension cell culture. Ions with a higher charge and smaller solvated ion radius, such as sulfate ions, have higher retention in an ion exchanger because of their greater degree of coulombic interactions (15).…”

Section: Resultsmentioning

confidence: 99%

“…The column was washed with 2 ml of the same buffer, and samples were eluted stepwise with 2.0-ml aliquots of 200 mM, 400 mM, and 600 mM ammonium acetate (pH 7.5). The 600 mM fraction was analyzed by LC-MS (LCQ Deca XP-plus; Thermo Electron, Waltham, MA) to search for sulfated peptides as described previously (15). A 16.7-min peak was collected and analyzed by automated Edman degradation by using an ABI Procise 491 protein sequencer.…”

Section: Methodsmentioning

confidence: 99%

“…We previously developed a procedure for specifically enriching low-concentration sulfated peptides from complex peptide mixtures based on an ion-selective interaction of sulfated peptides with anion exchangers (15). By using this procedure, we searched for sulfated peptides in plant cell culture medium, which predominantly contains secreted peptides and proteins produced by individual cells.…”

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confidence: 99%

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Tyrosine-sulfated glycopeptide involved in cellular proliferation and expansion in Arabidopsis

Amano

Tsubouchi²,

Shinohara³

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

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292

338

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Posttranslational modification can confer special functions to peptides. Based on exhaustive liquid chromatography mass spectrometry analysis targeting tyrosine-sulfated peptides, we identified an 18-aa tyrosine-sulfated glycopeptide in Arabidopsis cell suspension culture medium. This peptide, which we named PSY1, significantly promotes cellular proliferation and expansion at nanomolar concentrations. PSY1 is widely expressed in various Arabidopsis tissues, including shoot apical meristem, and is highly up-regulated by wounding. Perception of PSY1 depends on At1g72300, which is a leucine-rich repeat receptor kinase (LRR-RK) whose two paralogs are involved in the perception of phytosulfokine (PSK), which is a 5-aa tyrosine-sulfated peptide that primarily promotes cellular proliferation. Multiple loss-of-function mutations in these three paralogous LRR-RKs significantly enhanced phenotypes, compared with single disruptants, suggesting that these LRR-RKs have overlapping functions. Triple mutations in these LRR-RKs resulted in dwarfism because of decreases in cell number and cell size and caused insufficiency in tissue repair after wounding. The present results suggest that this paralogous LRR-RK family integrates growth-promoting signals mediated by two structurally distinct sulfated peptides: PSY1 and PSK.tyrosine sulfation ͉ leucine-rich repeat ͉ peptide hormone ͉ posttranslational modification ͉ receptor-like kinase

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

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Tyrosine-sulfated glycopeptide involved in cellular proliferation and expansion in Arabidopsis

Amano

Tsubouchi²,

Shinohara³

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

292

338

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“…Sulfate ions have a higher charge and a smaller ion radius, and are highly retained on anion-exchange resin relative to nonsulfated peptides [151]. These peptides are found in suspension cell media, which is a rich source for secreted peptides and proteins.…”

Section: Isolation Of Tyrosine-sulfated Peptidesmentioning

confidence: 99%

Plant Peptide Signals

Narváez-Vásquez

Orozco-Cárdenas

Pearce

2009

Amino Acids, Peptides and Proteins in Organic Chemistry

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“…For tyrosine phosphorylation, immunoprecipitation-based enrichment using anti-phosphotyrosine antibody has been the standard method [22,23]. As for the tyrosine O-sulfation, electron capture dissociation [24] and metastable atom-activated dissociation [25] as well as enrichment using anion exchange resin [26] have been employed. Recently, a new approach taking advantage of the labiality of the sulfate group in sulfotyrosine, easily detached under MS [27] and MS/MS conditions [27][28][29] has been reported by Yu et al for analysis of tyrosine O-sulfation [30].…”

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confidence: 99%

Simultaneous Identification of Tyrosine Phosphorylation and Sulfation Sites Utilizing Tyrosine-Specific Bromination

Kim

Song

Kim

2011

J. Am. Soc. Mass Spectrom.

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Tyrosine phosphorylation and sulfation play many key roles in the cell. Isobaric phosphotyrosine and sulfotyrosine residues in peptides were determined by mass spectrometry using phosphatase or sulfatase to remove the phosphate or the sulfate group. Unique Br signature was introduced to the resulting tyrosine residues by incubation with 32% HBr at −20°C for 20 min. MS/MS analysis of the brominated peptide enabled unambiguous determination of the phosphotyrosine and the sulfotyrosine sites. When phosphotyrosine and sulfotyrosine as well as free tyrosine were present in the same peptide, they could be determined simultaneously using either phosphatase or sulfatase following acetylation of the free tyrosine.

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Ion-selective enrichment of tyrosine-sulfated peptides from complex protein digests

Cited by 24 publications

References 26 publications

Tyrosine-sulfated glycopeptide involved in cellular proliferation and expansion in Arabidopsis

Tyrosine-sulfated glycopeptide involved in cellular proliferation and expansion in Arabidopsis

Plant Peptide Signals

Simultaneous Identification of Tyrosine Phosphorylation and Sulfation Sites Utilizing Tyrosine-Specific Bromination

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