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Jasmonate signalling in Arabidopsis involves SGT1b-HSP70-HSP90 chaperone complexes.
Zhang, Xue-Cheng; Millet, Yves A; Cheng, Zhenyu; Bush, Jenifer; Ausubel, Frederick M.
Afiliación
  • Zhang XC; Department of Genetics, Harvard Medical School, Boston, Massachusetts 02115, USA; Department of Molecular Biology, Massachusetts General Hospital, Boston, Massachusetts 02114, USA.
  • Millet YA; Department of Genetics, Harvard Medical School, Boston, Massachusetts 02115, USA; Department of Molecular Biology, Massachusetts General Hospital, Boston, Massachusetts 02114, USA.
  • Cheng Z; Department of Genetics, Harvard Medical School, Boston, Massachusetts 02115, USA; Department of Molecular Biology, Massachusetts General Hospital, Boston, Massachusetts 02114, USA.
  • Bush J; Department of Molecular Biology, Massachusetts General Hospital, Boston, Massachusetts 02114, USA.
  • Ausubel FM; Department of Genetics, Harvard Medical School, Boston, Massachusetts 02115, USA; Department of Molecular Biology, Massachusetts General Hospital, Boston, Massachusetts 02114, USA.
Nat Plants ; 12015.
Article en En | MEDLINE | ID: mdl-27054042
ABSTRACT
Plant hormones play pivotal roles in growth, development and stress responses. Although it is essential to our understanding of hormone signalling, how plants maintain a steady state level of hormone receptors is poorly understood. We show that mutation of the Arabidopsis thaliana co-chaperone SGT1b impairs responses to the plant hormones jasmonate, auxin and gibberellic acid, but not brassinolide and abscisic acid, and that SGT1b and its homologue SGT1a are involved in maintaining the steady state levels of the F-box proteins COI1 and TIR1, receptors for jasmonate and auxin, respectively. The association of SGT1b with COI1 is direct and is independent of the Arabidopsis SKP1 protein, ASK1. We further show that COI1 is a client protein of SGT1b-HSP70-HSP90 chaperone complexes and that the complexes function in hormone signalling by stabilizing the COI1 protein. This study extends the SGT1b-HSP90 client protein list and broadens the functional scope of SGT1b-HSP70-HSP90 chaperone complexes.

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Idioma: En Revista: Nat Plants Año: 2015 Tipo del documento: Article País de afiliación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Idioma: En Revista: Nat Plants Año: 2015 Tipo del documento: Article País de afiliación: Estados Unidos