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<jats:title>Abstract</jats:title><jats:sec> <jats:title>Main conclusion</jats:title> <jats:p><jats:bold>The post-transcriptional gene regulatory pathway and small RNA pathway play important roles in regulating the rapid and long-term response of Rhododendron moulmainense to high-temperature stress.</jats:bold></jats:p> </jats:sec><jats:sec> <jats:title>Abstract</jats:title> <jats:p>The Rhododendron plays an important role in maintaining ecological balance. However, it is difficult to domesticate for use in urban ecosystems due to their strict optimum growth temperature condition, and its evolution and adaptation are little known. Here, we combined transcriptome and small RNAome to reveal the rapid response and long-term adaptability regulation strategies in <jats:italic>Rhododendron moulmainense</jats:italic> under high-temperature stress. The post-transcriptional gene regulatory pathway plays important roles in stress response, in which the protein folding pathway is rapidly induced at 4 h after heat stress, and alternative splicing plays an important role in regulating gene expression at 7 days after heat stress. The chloroplasts oxidative damage is the main factor inhibiting photosynthesis efficiency. Through WGCNA analysis, we identified gene association patterns and potential key regulatory genes responsible for maintaining the ROS steady-state under heat stress. Finally, we found that the sRNA synthesis pathway is induced under heat stress. Combined with small RNAome, we found that more miRNAs are significantly changed under long-term heat stress. Furthermore, MYBs might play a central role in target gene interaction network of differentially expressed miRNAs in <jats:italic>R. moulmainense</jats:italic> under heat stress. MYBs are closely related to ABA, consistently, ABA synthesis and signaling pathways are significantly inhibited, and the change in stomatal aperture is not obvious under heat stress. Taken together, we gained valuable insights into the transplantation and long-term conservation domestication of <jats:italic>Rhododendron</jats:italic>, and provide genetic resources for genetic modification and molecular breeding to improve heat resistance in <jats:italic>Rhododendron</jats:italic>.</jats:p> </jats:sec>

<jats:title>Abstract</jats:title><jats:sec> <jats:title>Main conclusion</jats:title> <jats:p>Hydroxy(phenyl)pyruvic acid reductase from <jats:italic>Actaea racemosa</jats:italic> catalyzes dual reactions in reducing 4-hydroxyphenylpyruvic acid as well as β-hydroxypyruvic acid. It thus qualifies to be part of fukinolic and cimicifugic acid biosynthesis and also photorespiration.</jats:p> </jats:sec><jats:sec> <jats:title>Abstract</jats:title> <jats:p>The accumulation of fukinolic acid and cimicifugic acids is mainly restricted to <jats:italic>Actaea racemosa</jats:italic> (Ranunculaceae) and other species of the genus <jats:italic>Actaea</jats:italic>/<jats:italic>Cimicifuga</jats:italic>. Cimicifugic and fukinolic acids are composed of a hydroxycinnamic acid part esterified with a benzyltartaric acid moiety. The biosynthesis of the latter is unclear. We isolated cDNA encoding a hydroxy(phenyl)pyruvic acid reductase (GenBank OR393286) from suspension-cultured material of <jats:italic>A. racemosa</jats:italic> (ArH(P)PR) and expressed it in <jats:italic>E. coli</jats:italic> for protein production. The heterologously synthesized enzyme had a mass of 36.51 kDa and catalyzed the NAD(P)H-dependent reduction of 4-hydroxyphenylpyruvic acid to 4-hydroxyphenyllactic acid or β-hydroxypyruvic acid to glyceric acid, respectively. The optimal temperature was at 38 °C and the pH optimum at pH 7.5. NADPH is the preferred cosubstrate (K<jats:sub>m</jats:sub> 23 ± 4 µM). Several substrates are accepted by ArH(P)PR with β-hydroxypyruvic acid (K<jats:sub>m</jats:sub> 0.26 ± 0.12 mM) followed by 4-hydroxyphenylpyruvic acid (K<jats:sub>m</jats:sub> 1.13 ± 0.12 mM) as the best ones. Thus, ArH(P)PR has properties of β-hydroxypyruvic acid reductase (involved in photorespiration) as well as hydroxyphenylpyruvic acid reductase (possibly involved in benzyltartaric acid formation).</jats:p> </jats:sec>