A chemical reporter for protein AMPylation

Markus Grammel, Phi Luong, Kim Orth, Howard C. Hang

Research output: Contribution to journalArticle

42 Citations (Scopus)

Abstract

Protein AMPylation is an emerging post-translational modification, which plays key roles in bacterial pathogenesis and cell biology. Enzymes with AMPylation activity, referred to as AMPylators, have been identified in several bacterial pathogens and eukaryotes. To facilitate the study of this unique modification, we developed an alkynyl chemical reporter for detection and identification of protein AMPylation substrates. Covalent functionalization of AMPylation substrates with the alkynyl reporter in lieu of adenylyl 5′-monophosphate (AMP) allows their subsequent bioorthogonal ligation with azide-fluorescent dyes or affinity enrichment tags. We show that this chemical reporter is transferred by a range of AMPylators onto their cognate protein substrates and allows rapid detection and identification of AMPylated substrates.

Original languageEnglish (US)
Pages (from-to)17103-17105
Number of pages3
JournalJournal of the American Chemical Society
Volume133
Issue number43
DOIs
StatePublished - Nov 2 2011

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Proteins
Substrates
Azides
Cytology
Post Translational Protein Processing
Eukaryota
Fluorescent Dyes
Ligation
Cell Biology
Pathogens
Enzymes
Dyes

ASJC Scopus subject areas

  • Chemistry(all)
  • Catalysis
  • Biochemistry
  • Colloid and Surface Chemistry

Cite this

A chemical reporter for protein AMPylation. / Grammel, Markus; Luong, Phi; Orth, Kim; Hang, Howard C.

In: Journal of the American Chemical Society, Vol. 133, No. 43, 02.11.2011, p. 17103-17105.

Research output: Contribution to journalArticle

Grammel, Markus ; Luong, Phi ; Orth, Kim ; Hang, Howard C. / A chemical reporter for protein AMPylation. In: Journal of the American Chemical Society. 2011 ; Vol. 133, No. 43. pp. 17103-17105.
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