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Two P450 reductases from cotton were isolated and characterized. Their
in vitro activities were stimulated by low ionic strength.
GhCPR1 of Class I showed a constitutive expression pattern, and
GhCPR2 of Class II was inducible by elicitation.
Cytochrome P450 monooxygenases (P450s) are commonly involved in biosynthesis of endogenous compounds and catabolism of xenobiotics, and their activities rely on a partner enzyme, cytochrome P450 reductase (CPR, E.C.1.6.2.4). Two CPR cDNAs, GhCPR1 and GhCPR2, were isolated from cotton (
Gossypium hirsutum). They are 71% identical to each other at the amino acid sequence level and belong to the Class I and II of dicotyledonous CPRs, respectively. The recombinant enzymes reduced cytochrome
c, ferricyanide and dichlorophenolindophenol (DCPIP) in an NADPH-dependent manner, and supported the activity of CYP73A25, a cinnamate 4-hydroxylase of cotton. Both
GhCPR genes were widely expressed in cotton tissues, with a reduced expression level of
GhCPR2 in the glandless cotton cultivar. Expression of
GhCPR2, but not
GhCPR1, was inducible by mechanical wounding and elicitation, indicating that the
GhCPR2 is more related to defense reactions, including biosynthesis of secondary metabolites.