The Arabidopsis thaliana SERK1 kinase domain spontaneously refolds to an active state in vitro

M. aan den Toorn, M.M.E. Huijbers, S.C. de Vries, C.P.M. van Mierlo

Research output: Contribution to journalArticleAcademicpeer-review

4 Citations (Scopus)

Abstract

Auto-phosphorylating kinase activity of plant leucine-rich-repeat receptor-like kinases (LRR-RLK's) needs to be under tight negative control to avoid unscheduled activation. One way to achieve this would be to keep these kinase domains as intrinsically disordered protein (IDP) during synthesis and transport to its final location. Subsequent folding, which may depend on chaperone activity or presence of interaction partners, is then required for full activation of the kinase domain. Bacterially produced SERK1 kinase domain was previously shown to be an active Ser/Thr kinase. SERK1 is predicted to contain a disordered region in kinase domains X and XI. Here, we show that loss of structure of the SERK1 kinase domain during unfolding is intimately linked to loss of activity. Phosphorylation of the SERK1 kinase domain neither changes its structure nor its stability. Unfolded SERK1 kinase has no autophosphorylation activity and upon removal of denaturant about one half of the protein population spontaneously refolds to an active protein in vitro. Thus, neither chaperones nor interaction partners are required during folding of this protein to its catalytically active state.
Original languageEnglish
Article numbere50907
JournalPLoS ONE
Volume7
Issue number12
DOIs
Publication statusPublished - 2012

Keywords

  • embryogenesis receptor kinase-1
  • intrinsically disordered proteins
  • smooth-muscle myosin
  • to-order transition
  • molecular recognition
  • signal-transduction
  • structural basis
  • activation loop
  • gras proteins
  • phosphorylation

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