The phytosulfokine (PSK) receptor is capable of guanylate cyclase activity and enabling cyclic GMP-dependent signaling in plants
Wheeler, Janet I.
Thompson, Philip E.
Gehring, Christoph A
Irving, Helen R.
KAUST DepartmentBiological and Environmental Sciences and Engineering (BESE) Division
Molecular Signalling Group
Online Publication Date2011-04-19
Print Publication Date2011-06-24
Permanent link to this recordhttp://hdl.handle.net/10754/561756
MetadataShow full item record
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.
SponsorsThis work was supported by the Australian Research Council Discovery funding scheme (Project Number DP0878194) and by the National Research Fund South Africa.
JournalJournal of Biological Chemistry
PubMed Central IDPMC3121402
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