The chemical compound 'Heatin' stimulates hypocotyl elongation and interferes with the Arabidopsis NIT1-subfamily of nitrilases.
Aldehyde Oxidase
/ genetics
Aminohydrolases
/ genetics
Apomorphine
/ analogs & derivatives
Arabidopsis
/ drug effects
Arabidopsis Proteins
/ genetics
Enzyme Inhibitors
/ administration & dosage
Gene Expression Regulation, Plant
/ drug effects
Herbicides
/ pharmacology
Hypocotyl
/ drug effects
Indoleacetic Acids
Molecular Structure
Picloram
/ pharmacology
Structure-Activity Relationship
Transcriptome
/ drug effects
1-iminomethyl-2-naphthol
Arabidopsis
Heatin
IAN
NIT1-subfamily
PIF4
aldehyde oxidase
chemical genetics
indole-3-acetonitrile
nitrilases
thermomorphogenesis
Journal
The Plant journal : for cell and molecular biology
ISSN: 1365-313X
Titre abrégé: Plant J
Pays: England
ID NLM: 9207397
Informations de publication
Date de publication:
06 2021
06 2021
Historique:
received:
06
01
2021
accepted:
22
03
2021
pubmed:
27
3
2021
medline:
16
12
2021
entrez:
26
3
2021
Statut:
ppublish
Résumé
Temperature passively affects biological processes involved in plant growth. Therefore, it is challenging to study the dedicated temperature signalling pathways that orchestrate thermomorphogenesis, a suite of elongation growth-based adaptations that enhance leaf-cooling capacity. We screened a chemical library for compounds that restored hypocotyl elongation in the pif4-2-deficient mutant background at warm temperature conditions in Arabidopsis thaliana to identify modulators of thermomorphogenesis. The small aromatic compound 'Heatin', containing 1-iminomethyl-2-naphthol as a pharmacophore, was selected as an enhancer of elongation growth. We show that ARABIDOPSIS ALDEHYDE OXIDASES redundantly contribute to Heatin-mediated hypocotyl elongation. Following a chemical proteomics approach, the members of the NITRILASE1-subfamily of auxin biosynthesis enzymes were identified among the molecular targets of Heatin. Our data reveal that nitrilases are involved in promotion of hypocotyl elongation in response to high temperature and Heatin-mediated hypocotyl elongation requires the NITRILASE1-subfamily members, NIT1 and NIT2. Heatin inhibits NIT1-subfamily enzymatic activity in vitro and the application of Heatin accordingly results in the accumulation of NIT1-subfamily substrate indole-3-acetonitrile in vivo. However, levels of the NIT1-subfamily product, bioactive auxin (indole-3-acetic acid), were also significantly increased. It is likely that the stimulation of hypocotyl elongation by Heatin might be independent of its observed interaction with NITRILASE1-subfamily members. However, nitrilases may contribute to the Heatin response by stimulating indole-3-acetic acid biosynthesis in an indirect way. Heatin and its functional analogues present novel chemical entities for studying auxin biology.
Identifiants
pubmed: 33768644
doi: 10.1111/tpj.15250
pmc: PMC8360157
doi:
Substances chimiques
10,11-dihydroxy-N-n-propylnorapomorphine
0
Arabidopsis Proteins
0
Enzyme Inhibitors
0
Herbicides
0
Indoleacetic Acids
0
AAO1 protein, Arabidopsis
EC 1.2.3.1
Aldehyde Oxidase
EC 1.2.3.1
Aminohydrolases
EC 3.5.4.-
nitrilase
EC 3.5.5.1
Apomorphine
N21FAR7B4S
Picloram
O7437X49DW
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1523-1540Subventions
Organisme : H2020 European Research Council
ID : 616449
Organisme : H2020 European Research Council
ID : 258413
Organisme : Swedish Research Council
Organisme : Netherlands Organisation for Scientific research (NWO)
ID : 831.13.002
Organisme : Deutsche Forschungsgemeinschaft (DFG)
ID : INST 20876/127-1
Organisme : BBSRC
ID : BB/R017913/1
Organisme : BBSRC
ID : BB/S003193/1
Organisme : Swedish Metabolomics Centre for the Use of Instrumentation
Organisme : Knut and Alice Wallenberg Foundation (KAW)
Organisme : Ministry of Education Youth and Sports of the Czech Republic
ID : CZ.02.1.01/0.0/0.0/16_019/0000827
Organisme : Swedish Foundation for Strategic Research
Informations de copyright
© 2021 The Authors. The Plant Journal published by Society for Experimental Biology and John Wiley & Sons Ltd.
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