The phytosulfokine (PSK) receptor is capable of guanylate cyclase activity and enabling cyclic GMP-dependent signaling in plants

Handle URI:
http://hdl.handle.net/10754/561756
Title:
The phytosulfokine (PSK) receptor is capable of guanylate cyclase activity and enabling cyclic GMP-dependent signaling in plants
Authors:
Kwezi, Lusisizwe; Ruzvidzo, Oziniel; Wheeler, Janet I.; Govender, Kershini; Iacuone, Sylvana; Thompson, Philip E.; Gehring, Christoph A. ( 0000-0003-4355-4591 ) ; Irving, Helen R.
Abstract:
Phytosulfokines (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.
KAUST Department:
Biological and Environmental Sciences and Engineering (BESE) Division; Bioscience Program; Molecular Signalling Group
Publisher:
American Society for Biochemistry and Molecular Biology
Journal:
Journal of Biological Chemistry
Issue Date:
19-Apr-2011
DOI:
10.1074/jbc.M110.168823
PubMed ID:
21504901
PubMed Central ID:
PMC3121402
Type:
Article
ISSN:
00219258
Sponsors:
This work was supported by the Australian Research Council Discovery funding scheme (Project Number DP0878194) and by the National Research Fund South Africa.
Additional Links:
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3121402
Appears in Collections:
Articles; Bioscience Program; Biological and Environmental Sciences and Engineering (BESE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorKwezi, Lusisizween
dc.contributor.authorRuzvidzo, Ozinielen
dc.contributor.authorWheeler, Janet I.en
dc.contributor.authorGovender, Kershinien
dc.contributor.authorIacuone, Sylvanaen
dc.contributor.authorThompson, Philip E.en
dc.contributor.authorGehring, Christoph A.en
dc.contributor.authorIrving, Helen R.en
dc.date.accessioned2015-08-03T09:03:54Zen
dc.date.available2015-08-03T09:03:54Zen
dc.date.issued2011-04-19en
dc.identifier.issn00219258en
dc.identifier.pmid21504901en
dc.identifier.doi10.1074/jbc.M110.168823en
dc.identifier.urihttp://hdl.handle.net/10754/561756en
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.en
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.en
dc.publisherAmerican Society for Biochemistry and Molecular Biologyen
dc.relation.urlhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3121402en
dc.titleThe phytosulfokine (PSK) receptor is capable of guanylate cyclase activity and enabling cyclic GMP-dependent signaling in plantsen
dc.typeArticleen
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Divisionen
dc.contributor.departmentBioscience Programen
dc.contributor.departmentMolecular Signalling Groupen
dc.identifier.journalJournal of Biological Chemistryen
dc.identifier.pmcidPMC3121402en
dc.contributor.institutionMedicinal Chemistry and Drug Action, Monash Institute of Pharmaceutical Sciences, Monash University (Parkville Campus), 381 Royal Parade, Parkville, VIC 3052, Australiaen
dc.contributor.institutionDepartment of Biotechnology, University of the Western Cape, Bellville, 7535, South Africaen
dc.contributor.institutionDept. of Biological Sciences, North-West University, Private Bag X2046, Mmabatho 2735, South Africaen
kaust.authorGehring, Christoph A.en

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