In vitro assessment of guanylyl cyclase activity of plant receptor kinases

Misjudeen Raji, Chris Gehring*

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

4 Scopus citations

Abstract

Cyclic nucleotides such as 3′,5′-cyclic adenosine monophosphate (cAMP) and 3′,5′-cyclic guanosine monophosphate (cGMP) are increasingly recognized as key signaling molecules in plants, and a growing number of plant mononucleotide cyclases, both adenylate cyclases (ACs) and guanylate cyclases (GCs), have been reported. Catalytically active cytosolic GC domains have been shown to be part of many plant receptor kinases and hence directly linked to plant signaling and downstream cellular responses. Here we detail, firstly, methods to identify and express essential functional GC domains of receptor kinases, and secondly, we describe mass spectrometric methods to quantify cGMP generated by recombinant GCs from receptor kinases in vitro.

Original languageEnglish (US)
Title of host publicationMethods in Molecular Biology
PublisherHumana Press Inc.
Pages131-140
Number of pages10
DOIs
StatePublished - 2017

Publication series

NameMethods in Molecular Biology
Volume1621
ISSN (Print)1064-3745

Keywords

  • Cyclic nucleotides
  • Guanylate cyclase
  • HPLC
  • Nucleotide cyclase
  • Tandem mass spectrometry
  • cGMP

ASJC Scopus subject areas

  • Genetics
  • Molecular Biology

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