Structural conservation of WEE1 and its role in cell cycle regulation in plants

The WEE1 kinase is ubiquitous in plant development and negatively regulates the cell cycle through phosphorylations. However, analogies with the control of the human cell cycle by tyrosine- (Tyr-) phosphorylation of cyclin-dependent kinases (CDKs) are sometimes questioned. In this in silico study, w...

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Bibliographic Details
Published in:Scientific reports 2021-12, Vol.11 (1), p.23862-23862, Article 23862
Main Authors: Détain, A., Redecker, D., Leborgne-Castel, N., Ochatt, S.
Format: Article
Language:English
Subjects:
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Amino Acid Substitution
Bayesian analysis
Catalytic Domain
Cell Cycle
Conserved Sequence
Cyclin-dependent kinases
Cyclin-Dependent Kinases - chemistry
Cyclin-Dependent Kinases - genetics
Cyclin-Dependent Kinases - metabolism
Evolution, Molecular
Humanities and Social Sciences
Legumes
Life Sciences
Magnoliopsida - genetics
Magnoliopsida - metabolism
multidisciplinary
Phosphorylation
Phylogeny
Plant Proteins - chemistry
Plant Proteins - genetics
Plant Proteins - metabolism
Science
Science (multidisciplinary)
Sequence analysis
Tyrosine
Wee1 protein
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Summary:The WEE1 kinase is ubiquitous in plant development and negatively regulates the cell cycle through phosphorylations. However, analogies with the control of the human cell cycle by tyrosine- (Tyr-) phosphorylation of cyclin-dependent kinases (CDKs) are sometimes questioned. In this in silico study, we assessed the structural conservation of the WEE1 protein in the plant kingdom with a particular focus on agronomically valuable plants, the legume crops. We analyzed the phylogenetic distribution of amino-acid sequences among a large number of plants by Bayesian analysis that highlighted the general conservation of WEE1 proteins. A detailed sequence analysis confirmed the catalytic potential of WEE1 proteins in plants. However, some substitutions of an arginine and a glutamate at the entrance of the catalytic pocket, illustrated by 3D structure predictions, challenged the specificity of this protein toward the substrate and Tyr-phosphorylation compared to the human WEE1. The structural differences, which could be responsible for the loss of specificity between human and plants, are highlighted and suggest the involvement of plant WEE1 in more cell regulation processes.
ISSN:2045-2322
2045-2322
DOI:10.1038/s41598-021-03268-x