ArticlePlant biotechnology journal2026
Metabolic Enzyme MeHNL11 Regulates MeCAS1b Transcription for Cyanide Reutilization in Response to Nitrate Deficiency in Cassava.
Article in Plant biotechnology journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Cassava (Manihot esculenta Crantz) exhibits exceptional tolerance to infertile soils and contains abundant cyanogenic glucosides (CGs). Previous research has indicated that CGs can serve as a significant reservoir of organic nitrogen in plants. However, the extent to which its high-CG content contributes to efficient nitrogen utilisation and adaptation to low nitrogen (N) in cassava remains to be further elucidated. This study represents the first identification of MeHNL11 as a bifunctional protein. In response to N deficiency, the hydroxynitrile lyase activity of MeHNL11 promotes the generation and accumulation of cyanide and the Cys245 residue of MeHNL11 is critical for its nuclear oligomerization, in which the protein functions as a transcription factor. Following the cyanide transmission into the nucleus, the oligomeric form of MeHNL11 dissociates into monomers, leading to a dramatic upregulation of MeCAS1b transcription. This regulatory mechanism helps sustain intracellular cyanide homeostasis within cassava and facilitates the synthesis of primary N metabolites, thereby alleviating N deficiency. The exogenous application of the cyanide antidote hydroxocobalamin (COB) inhibited cyanide assimilation by MeCAS1b, leading to exacerbated N deficiency symptoms, such as leaf yellowing and a significant reduction in the contents of NH
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