Identification of selenoprotein O substrates using a biotinylated ATP analog

Meghomukta Mukherjee, Anju Sreelatha

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

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 publicationMethods in Enzymology
PublisherAcademic Press Inc.
DOIs
StateAccepted/In press - 2021

Publication series

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

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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