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dc.contributor.authorKwezi, Lusisizwe
dc.contributor.authorRuzvidzo, Oziniel
dc.contributor.authorWheeler, Janet I.
dc.contributor.authorGovender, Kershini
dc.contributor.authorIacuone, Sylvana
dc.contributor.authorThompson, Philip E.
dc.contributor.authorGehring, Christoph A
dc.contributor.authorIrving, Helen R.
dc.date.accessioned2015-08-03T09:03:54Z
dc.date.available2015-08-03T09:03:54Z
dc.date.issued2011-04-19
dc.identifier.citationKwezi, L., Ruzvidzo, O., Wheeler, J. I., Govender, K., Iacuone, S., Thompson, P. E., … Irving, H. R. (2011). The Phytosulfokine (PSK) Receptor Is Capable of Guanylate Cyclase Activity and Enabling Cyclic GMP-dependent Signaling in Plants. Journal of Biological Chemistry, 286(25), 22580–22588. doi:10.1074/jbc.m110.168823
dc.identifier.issn00219258
dc.identifier.pmid21504901
dc.identifier.doi10.1074/jbc.M110.168823
dc.identifier.urihttp://hdl.handle.net/10754/561756
dc.description.abstractPhytosulfokines (PSKs) are sulfated pentapeptides that stimulate plant growth and differentiation mediated by the PSK receptor (PSKR1), which is a leucine-rich repeat receptor-like kinase. We identified a putative guanylate cyclase (GC) catalytic center in PSKR1 that is embedded within the kinase domain and hypothesized that the GC works in conjunction with the kinase in downstream PSK signaling. We expressed the recombinant complete kinase (cytoplasmic) domain of AtPSKR1 and show that it has serine/threonine kinase activity using the Ser/Thr peptide 1 as a substrate with an approximate Km of 7.5 μM and Vmax of 1800 nmol min-1 mg-1 of protein. This same recombinant protein also has GC activity in vitro that is dependent on the presence of either Mg2+ or Mn2+. Overexpression of the full-length AtPSKR1 receptor in Arabidopsis leaf protoplasts raised the endogenous basal cGMP levels over 20-fold, indicating that the receptor has GC activity in vivo. In addition, PSK-α itself, but not the non-sulfated backbone, induces rapid increases in cGMP levels in protoplasts. Together these results indicate that the PSKR1 contains dual GC and kinase catalytic activities that operate in vivo and that this receptor constitutes a novel class of enzymes with overlapping catalytic domains. © 2011 by The American Society for Biochemistry and Molecular Biology, Inc.
dc.description.sponsorshipThis work was supported by the Australian Research Council Discovery funding scheme (Project Number DP0878194) and by the National Research Fund South Africa.
dc.publisherAmerican Society for Biochemistry & Molecular Biology (ASBMB)
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3121402
dc.titleThe phytosulfokine (PSK) receptor is capable of guanylate cyclase activity and enabling cyclic GMP-dependent signaling in plants
dc.typeArticle
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Division
dc.contributor.departmentBioscience Program
dc.contributor.departmentMolecular Signalling Group
dc.identifier.journalJournal of Biological Chemistry
dc.identifier.pmcidPMC3121402
dc.contributor.institutionMedicinal Chemistry and Drug Action, Monash Institute of Pharmaceutical Sciences, Monash University (Parkville Campus), 381 Royal Parade, Parkville, VIC 3052, Australia
dc.contributor.institutionDepartment of Biotechnology, University of the Western Cape, Bellville, 7535, South Africa
dc.contributor.institutionDept. of Biological Sciences, North-West University, Private Bag X2046, Mmabatho 2735, South Africa
kaust.personGehring, Christoph A.
dc.date.published-online2011-04-19
dc.date.published-print2011-06-24


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