Accumulation of the Auxin Precursor Indole-3-Acetamide Curtails Growth through the Repression of Ribosome-Biogenesis and Development-Related Transcriptional Networks.
Beatriz Sánchez-ParraMarta-Marina Pérez-AlonsoPaloma Ortiz-GarcíaJosé Moya-CuevasMathias HentrichStephan PollmannPublished in: International journal of molecular sciences (2021)
The major auxin, indole-3-acetic acid (IAA), is associated with a plethora of growth and developmental processes including embryo development, expansion growth, cambial activity, and the induction of lateral root growth. Accumulation of the auxin precursor indole-3-acetamide (IAM) induces stress related processes by stimulating abscisic acid (ABA) biosynthesis. How IAM signaling is controlled is, at present, unclear. Here, we characterize the ami1rooty double mutant, that we initially generated to study the metabolic and phenotypic consequences of a simultaneous genetic blockade of the indole glucosinolate and IAM pathways in Arabidopsisthaliana. Our mass spectrometric analyses of the mutant revealed that the combination of the two mutations is not sufficient to fully prevent the conversion of IAM to IAA. The detected strong accumulation of IAM was, however, recognized to substantially impair seed development. We further show by genome-wide expression studies that the double mutant is broadly affected in its translational capacity, and that a small number of plant growth regulating transcriptional circuits are repressed by the high IAM content in the seed. In accordance with the previously described growth reduction in response to elevated IAM levels, our data support the hypothesis that IAM is a growth repressing counterpart to IAA.
Keyphrases
- genome wide
- transcription factor
- poor prognosis
- dna methylation
- acute myocardial infarction
- machine learning
- pregnant women
- percutaneous coronary intervention
- arabidopsis thaliana
- coronary artery disease
- single cell
- minimally invasive
- electronic health record
- copy number
- oxidative stress
- big data
- deep learning
- heat shock protein