Abstract
Aux/IAA proteins are short-lived nuclear proteins that repress expression of primary/early auxin response genes in protoplast transfection assays. Repression is thought to result from Aux/IAA proteins dimerizing with auxin response factor (ARF) transcriptional activators that reside on auxin-responsive promoter elements, referred to as AuxREs. Most Aux/IAA proteins contain four conserved domains, designated domains I, II, III, and IV. Domain II and domains III and IV play roles in protein stability and dimerization, respectively. A clear function for domain I had not been established. Results reported here indicate that domain I in Aux/IAA proteins is an active repression domain that is transferable and dominant over activation domains. An LxLxL motif within domain I is important for conferring repression. The dominance of Aux/IAA repression domains over activation domains in ARF transcriptional activators provides a plausible explanation for the repression of auxin response genes via ARF-Aux/IAA dimerization on auxin-responsive promoters.
MeSH Terms
Amino Acid Sequence
Arabidopsis Proteins/chemistry,genetics,metabolism
Binding Sites/genetics
DNA-Binding Proteins
Leucine/metabolism
Nuclear Proteins/chemistry,genetics,metabolism
Plant Proteins
Protein Interaction Mapping
Recombinant Fusion Proteins/genetics,metabolism
Repressor Proteins/genetics,metabolism
Trans-Activators/genetics,metabolism
Transcription Factors/genetics,metabolism
Chemicals
AXR3 protein, Arabidopsis
Arabidopsis Proteins
DNA-Binding Proteins
Nuclear Proteins
Plant Proteins
Recombinant Fusion Proteins
Repressor Proteins
Trans-Activators
Transcription Factors
superman protein, Arabidopsis
ethylene-responsive element binding protein
Leucine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Tiwari Shiv B
Department of Biochemistry, University of Missouri, Columbia, Missouri 65211, USA.
Hagen Gretchen
Guilfoyle Tom J
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