IAA1 protein is encoded by AXR5 and is a substrate of SCFTIR1

Summary Recent studies of auxin response have focused on the functions of three sets of proteins: the auxin (Aux) response factors (ARFs), the Aux/IAAs, and the F‐box protein TIR1. The ARF proteins bind DNA and directly activate or repress transcription of target genes while the Aux/IAA proteins rep...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:The Plant journal : for cell and molecular biology 2004-12, Vol.40 (5), p.772-782
Hauptverfasser: Yang, X, Lee, S, So, J.H, Dharmasiri, S, Dharmasiri, N, Ge, L, Jensen, C, Hangarter, R, Hobbie, L, Estelle, M
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
Beschreibung
Zusammenfassung:Summary Recent studies of auxin response have focused on the functions of three sets of proteins: the auxin (Aux) response factors (ARFs), the Aux/IAAs, and the F‐box protein TIR1. The ARF proteins bind DNA and directly activate or repress transcription of target genes while the Aux/IAA proteins repress ARF function. TIR1 is part of a ubiquitin protein ligase required for degradation of Aux/IAA proteins. Here we report the isolation and characterization of a novel mutant of Arabidopsis called axr5‐1. Mutant plants are resistant to auxin and display a variety of auxin‐related growth defects including defects in root and shoot tropisms. Further, the axr5‐1 mutation results in a decrease in auxin‐regulated transcription. The molecular cloning of AXR5 revealed that the gene encodes the IAA1 protein, a member of the Aux/IAA family of proteins. AXR5 is expressed throughout plant development consistent with the pleiotropic mutant phenotype. The axr5‐1 mutation results in an amino acid substitution in conserved domain II of the protein, similar to gain‐of‐function mutations recovered in other members of this gene family. Biochemical studies show that IAA1/AXR5 interacts with TIR1 in an auxin‐dependent manner. The mutation prevents this interaction suggesting that the mutant phenotype is caused by the accumulation of IAA1/AXR5. Our results provide further support for a model in which most members of the Aux/IAA family are targeted for degradation by SCFTIR1 in response to auxin.
ISSN:0960-7412
1365-313X
DOI:10.1111/j.1365-313x.2004.02254.x