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Soybean nodule autoregulation receptor kinase phosphorylates two kinase-associated protein phosphatases in Vitro

Miyahara, Akira; Hirani, Tripty A; Oakes, Marie; Kereszt, Attila; Kobe, Bostjan; Djordjevic, Michael; Gresshoff, Peter

Description

The NARK (nodule autoregulation receptor kinase) gene, a negative regulator of cell proliferation in nodule primordia in several legumes, encodes a receptor kinase that consists of an extracellular leucine-rich repeat and an intracellular serine/threonine protein kinase domain. The putative catalytic domain of NARK was expressed and purified as a maltose-binding or a glutathione S-transferase fusion protein in Escherichia coli. The recombinant NARK proteins showed autophosphorylation activity...[Show more]

dc.contributor.authorMiyahara, Akira
dc.contributor.authorHirani, Tripty A
dc.contributor.authorOakes, Marie
dc.contributor.authorKereszt, Attila
dc.contributor.authorKobe, Bostjan
dc.contributor.authorDjordjevic, Michael
dc.contributor.authorGresshoff, Peter
dc.date.accessioned2015-12-10T22:54:42Z
dc.date.available2015-12-10T22:54:42Z
dc.identifier.issn0021-9258
dc.identifier.urihttp://hdl.handle.net/1885/59752
dc.description.abstractThe NARK (nodule autoregulation receptor kinase) gene, a negative regulator of cell proliferation in nodule primordia in several legumes, encodes a receptor kinase that consists of an extracellular leucine-rich repeat and an intracellular serine/threonine protein kinase domain. The putative catalytic domain of NARK was expressed and purified as a maltose-binding or a glutathione S-transferase fusion protein in Escherichia coli. The recombinant NARK proteins showed autophosphorylation activity in vitro. Several regions of the NARK kinase domain were shown by mass spectrometry to possess phosphoresidues. The kinase-inactive protein K724E failed to autophosphorylate, as did three other proteins corresponding to phenotypically detected mutants defective in whole plant autoregulation of nodulation. A wild-type NARK fusion protein transphosphorylated a kinase-inactive mutant NARK fusion protein, suggesting that it is capable of intermolecular autophosphorylation in vitro. In addition, Ser-861 and Thr-963 in the NARK kinase catalytic domain were identified as phosphorylation sites through site-directed mutagenesis. The genes coding for the kinase-associated protein phosphatases KAPP1 and KAPP2, two putative interacting components of NARK, were isolated. NARK kinase domain phosphorylated recombinant KAPP proteins in vitro. Autophosphorylated NARK kinase domain was, in turn, dephosphorylated by both KAPP1 and KAPP2. Our results suggest a model for signal transduction involving NARK in the control of nodule development.
dc.publisherAmerican Society for Biochemistry and Molecular Biology Inc
dc.sourceJournal of Biological Chemistry
dc.subjectKeywords: Amino acids; Cell proliferation; Escherichia coli; High performance liquid chromatography; Mass spectrometry; Phosphorylation; Programming theory; Proteins; Signal transduction; Autoregulation; Catalytic domains; Extracellular; Fusion proteins; Genes codi
dc.titleSoybean nodule autoregulation receptor kinase phosphorylates two kinase-associated protein phosphatases in Vitro
dc.typeJournal article
local.description.notesImported from ARIES
local.identifier.citationvolume283
dc.date.issued2008
local.identifier.absfor060705 - Plant Physiology
local.identifier.ariespublicationu9204316xPUB506
local.type.statusPublished Version
local.contributor.affiliationMiyahara, Akira, University of Queensland
local.contributor.affiliationHirani, Tripty A, University of Queensland
local.contributor.affiliationOakes, Marie, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationKereszt, Attila, University of Queensland
local.contributor.affiliationKobe, Bostjan, St Vincent's Institute of Medical Research
local.contributor.affiliationDjordjevic, Michael, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationGresshoff, Peter, University of Queensland
local.bibliographicCitation.issue37
local.bibliographicCitation.startpage25381
local.bibliographicCitation.lastpage25391
local.identifier.doi10.1074/jbc.M800400200
dc.date.updated2016-02-24T11:52:18Z
local.identifier.scopusID2-s2.0-54449091805
local.identifier.thomsonID000259012700033
CollectionsANU Research Publications

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