Identification of selenoprotein O substrates using a biotinylated ATP analog

Meghomukta Mukherjee, Anju Sreelatha

Research output: Chapter in Book/Report/Conference proceedingChapter

1 Scopus citations


Selenoprotein O is one of 25 human selenoproteins that incorporate the 21st amino acid selenocysteine. Recent studies have revealed a previously undocumented mechanism of redox regulation by which SelO protects cells from oxidative damage. SelO catalyzes the covalent addition of AMP from ATP to the hydroxyl side chain of protein substrates in a post translational modification known as AMPylation. Although AMPylation was discovered over 50 years ago, methods to detect and enrich substrates are limited. Here, we describe protocols to clone, purify, and identify the substrates of bacterial SelO using a biotinylated ATP analog. Identification of SelO substrates and the functional consequences of AMPylation will illuminate the significance of this evolutionarily conserved selenoprotein.

Original languageEnglish (US)
Title of host publicationSelenoprotein Structure and Function
EditorsEranthie Weerapana
PublisherAcademic Press Inc.
Number of pages22
ISBN (Print)9780323907354
StatePublished - Jan 2022

Publication series

NameMethods in Enzymology
ISSN (Print)0076-6879
ISSN (Electronic)1557-7988


  • AMPylation
  • Adenylylation
  • Mitochondria
  • Oxidative stress
  • Pseudokinase
  • SelenoO
  • ydiU

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


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