In Vitro Assessment of Guanylyl Cyclase Activity of Plant Receptor Kinases

Handle URI:
http://hdl.handle.net/10754/625598
Title:
In Vitro Assessment of Guanylyl Cyclase Activity of Plant Receptor Kinases
Authors:
Raji, Misjudeen; Gehring, Christoph A. ( 0000-0003-4355-4591 )
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.
KAUST Department:
Analytical Core Lab; Division of Biological & Environmental Science & Engineering, 4700 King Abdullah University of Science and Technology, Thuwal, 23955-6900, , Saudi Arabia
Citation:
Raji M, Gehring C (2017) In Vitro Assessment of Guanylyl Cyclase Activity of Plant Receptor Kinases. Plant Receptor Kinases: 131–140. Available: http://dx.doi.org/10.1007/978-1-4939-7063-6_13.
Publisher:
Springer New York
Journal:
Methods in Molecular Biology
Issue Date:
31-May-2017
DOI:
10.1007/978-1-4939-7063-6_13
Type:
Book Chapter
ISSN:
1064-3745; 1940-6029
Sponsors:
We are grateful to the KAUST Analytical Core Lab for supporting this project.
Additional Links:
https://link.springer.com/protocol/10.1007%2F978-1-4939-7063-6_13
Appears in Collections:
Analytical Core Lab; Book Chapters

Full metadata record

DC FieldValue Language
dc.contributor.authorRaji, Misjudeenen
dc.contributor.authorGehring, Christoph A.en
dc.date.accessioned2017-10-03T12:49:28Z-
dc.date.available2017-10-03T12:49:28Z-
dc.date.issued2017-05-31en
dc.identifier.citationRaji M, Gehring C (2017) In Vitro Assessment of Guanylyl Cyclase Activity of Plant Receptor Kinases. Plant Receptor Kinases: 131–140. Available: http://dx.doi.org/10.1007/978-1-4939-7063-6_13.en
dc.identifier.issn1064-3745en
dc.identifier.issn1940-6029en
dc.identifier.doi10.1007/978-1-4939-7063-6_13en
dc.identifier.urihttp://hdl.handle.net/10754/625598-
dc.description.abstractCyclic 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.en
dc.description.sponsorshipWe are grateful to the KAUST Analytical Core Lab for supporting this project.en
dc.publisherSpringer New Yorken
dc.relation.urlhttps://link.springer.com/protocol/10.1007%2F978-1-4939-7063-6_13en
dc.subjectcGMPen
dc.subjectCyclic nucleotidesen
dc.subjectGuanylate cyclaseen
dc.subjectHPLCen
dc.subjectNucleotide cyclaseen
dc.subjectTandem mass spectrometryen
dc.titleIn Vitro Assessment of Guanylyl Cyclase Activity of Plant Receptor Kinasesen
dc.typeBook Chapteren
dc.contributor.departmentAnalytical Core Laben
dc.contributor.departmentDivision of Biological & Environmental Science & Engineering, 4700 King Abdullah University of Science and Technology, Thuwal, 23955-6900, , Saudi Arabiaen
dc.identifier.journalMethods in Molecular Biologyen
kaust.authorRaji, Misjudeenen
kaust.authorGehring, Christoph A.en
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