ArticleThe Plant cell2024
Two pyridoxal phosphate homeostasis proteins are essential for management of the coenzyme pyridoxal 5'-phosphate in Arabidopsis.
Article in The Plant cell, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Targeted population genomics uncovers demographic history and genetic divergence in north American wild cranberry.Horticulture research · 2026Article
- PLP Homeostasis Protein Is Required for Efficient Maturation of Aromatic Amino Acid Aminotransferase in Salmonella enterica.Molecular microbiology · 2026Article
- Sulfur-Containing Amino Acids: The Conversion Process from Product to Substrate.International journal of molecular sciences · 2026Review
- Mutational analyses reveal PLP-independent functions at PipY, the cyanobacterial paradigm for pyridoxal-phosphate binding proteins.Scientific reports · 2026Article
- The ubiquitous pyridoxal 5'-phosphate-binding protein is also an RNA-binding protein.Protein science : a publication of the Protein Society · 2024Article
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Authors and funding
2 authors.
Funding
Abstract
Coenzyme management is important for homeostasis of the pool of active metabolic enzymes. The coenzyme pyridoxal 5'-phosphate (PLP) is involved in diverse enzyme reactions including amino acid and hormone metabolism. Regulatory proteins that contribute to PLP homeostasis remain to be explored in plants. Here, we demonstrate the importance of proteins annotated as PLP homeostasis proteins (PLPHPs) for controlling PLP in Arabidopsis (Arabidopsis thaliana). A systematic analysis indicates that while most organisms across kingdoms have a single PLPHP homolog, Angiosperms have two. PLPHPs from Arabidopsis bind PLP and exist as monomers, in contrast to reported PLP-dependent enzymes, which exist as multimers. Disrupting the function of both PLPHP homologs perturbs vitamin B6 (pyridoxine) content, inducing a PLP deficit accompanied by light hypersensitive root growth, unlike PLP biosynthesis mutants. Micrografting studies show that the PLP deficit can be relieved distally between shoots and roots. Chemical treatments probing PLP-dependent reactions, notably those for auxin and ethylene, provide evidence that PLPHPs function in the dynamic management of PLP. Assays in vitro show that Arabidopsis PLPHP can coordinate PLP transfer and withdrawal from other enzymes. This study thus expands our knowledge of vitamin B6 biology and highlights the importance of PLP coenzyme homeostasis in plants.
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