Author(s)

Laura M. C. Ades, Dorothy M. Morré, D. James Morré^*

Mor-NuCo, Inc., Purdue Research Park, West Lafayette, USA.

ENOX (ECTO-NOX) proteins of the external surface of the plasma membrane catalyze oxidation of both NADH and hydroquinones and protein disulfide-thiol interchange. They exhibit both prion-like and time-keeping (clock) properties. The oxidative and interchange activities alternate to generate a regular period of 24 min in length. Here we report the cloning, expression and characterization of a constitutive plant ENOX protein activated by both natural (Indole-3-acetic acid, IAA) and synthetic (2,4-dichlorophenoxyacetic acid, 2,4-D) auxin plant growth regulators with an optimum of about 1 μM, higher concentrations being less effective. The gene encoding the 213 amino acid protein (ABP20) is found in EMBL accession number U81162. Functional motifs characteristic of ENOX1 proteins, previously identified by site-directed mutagenesis, are present in the candidate auxin-activated ENOX (dNOX, ENOX5), including adenine nucleotide and copper binding motifs along with essential cysteines and a motif having homology with a previously identified auxin-binding motif. Periodicity was exhibited by both the oxidative and protein disulfide-thiol inter-change activities as is characteristic for other ENOX proteins. Activity was blocked by the ENOX2-specific quassinoid inhibitor glaucarubolone and other ENOX2 inhibitors but not by the ENOX1-specific quassinoid inhibitor simalikalactone D. Activity required both auxin and bound copper. The inactive auxin 2,3-D was without effects.

Auxin, Auxin-Binding Protein, 2, 4-D, dNOX, ENOX5: ECTO-NOX Proteins

Ades, L. , Morré, D. and Morré, D. (2014) Cloning and Characterization of a Candidate Auxin Plant Growth Regulator-Activated Cell Surface Hydroquinone (NADH) Oxidase. Advances in Biological Chemistry, 4, 415-427. doi: 10.4236/abc.2014.47047.