Intrinsic disorder and conformational coexistence in auxin coreceptors.
Aux/IAA
IDP
TIR1
auxin
disorder
Journal
Proceedings of the National Academy of Sciences of the United States of America
ISSN: 1091-6490
Titre abrégé: Proc Natl Acad Sci U S A
Pays: United States
ID NLM: 7505876
Informations de publication
Date de publication:
03 10 2023
03 10 2023
Historique:
medline:
9
11
2023
pubmed:
27
9
2023
entrez:
27
9
2023
Statut:
ppublish
Résumé
AUXIN/INDOLE 3-ACETIC ACID (Aux/IAA) transcriptional repressor proteins and the TRANSPORT INHIBITOR RESISTANT 1/AUXIN SIGNALING F-BOX (TIR1/AFB) proteins to which they bind act as auxin coreceptors. While the structure of TIR1 has been solved, structural characterization of the regions of the Aux/IAA protein responsible for auxin perception has been complicated by their predicted disorder. Here, we use NMR, CD and molecular dynamics simulation to investigate the N-terminal domains of the Aux/IAA protein IAA17/AXR3. We show that despite the conformational flexibility of the region, a critical W-P bond in the core of the Aux/IAA degron motif occurs at a strikingly high (1:1) ratio of
Identifiants
pubmed: 37756337
doi: 10.1073/pnas.2221286120
pmc: PMC10556615
doi:
Substances chimiques
Arabidopsis Proteins
0
Receptors, Cell Surface
0
Indoleacetic Acids
0
F-Box Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e2221286120Subventions
Organisme : Medical Research Council
ID : MR/T020652/1
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 094232
Pays : United Kingdom
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/L010623/1
Pays : United Kingdom
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/I532402/1
Pays : United Kingdom
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