Claim · model-written summary
The authors propose that AHLs interact with each other, themselves and other nuclear proteins to form complexes that modulate plant growth and development.
- Taxon
- Arabidopsis thaliana
Arabidopsis thalianat0 - Gene
- AHLse1
- Outcome
- plant growth and developmente1
Not reportedMaterialCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleTreatmentComparatorSettingDirectionValueQualifier
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
t0“Arabidopsis thaliana”
e1“We propose a molecular model where AHLs interact with each other and themselves, as well as other nuclear proteins, to form complexes which modulate plant growth and development”
Title
Jianfei Zhao; David S. Favero; Hao Peng; et al. Proceedings of the National Academy of Sciences 2013. doi:10.1073/pnas.1219277110
Other claims from this paper (9)
- Intervention effect Seedlings lacking both SOB3/AHL29 and ESC/AHL27 had a subtle long-hypocotyl phenotype compared with the wild type or either single-null mutant.
- Observation The missense allele sob3-6 conferred a dramatic long-hypocotyl phenotype in the light.
- Observation The sob3-6 allele encodes a protein with a disrupted AT-hook motif that abolishes binding to AT-rich DNA.
- Intervention effect A loss-of-function approach showed different but redundant contributions of additional AHL genes in suppressing hypocotyl elongation in the light.
- Observation AHL proteins interact with each other and themselves via the PPC/DUF296 domain.
- Observation AHLs also share interactions with other nuclear proteins such as transcription factors.
- Intervention effect Alteration of the conserved Gly-Arg-Phe-Glu-Ile-Leu region of the PPC/DUF296 domain abolished the physical interaction of SOB3/AHL29 with transcription factors.
- Intervention effect Alteration of that region also produced a dominant-negative allele in planta phenotypically similar to sob3-6.
- Mechanism The coordinated action of AHLs requires an AT-hook motif able to bind AT-rich DNA and a PPC/DUF296 domain containing a conserved Gly-Arg-Phe-Glu-Ile-Leu region.