Abstract: In the present disclosure, a yeast interactive plasmid of a detoxifying enzyme glucosinolate sulfatase (GSS1) is constructed based on a yeast two-hybrid system and then screened with an Arabidopsis thaliana-yeast library, and a plant protein zeaxanthin epoxidase aba1 that interacts with the GSS1 is obtained for the first time. A zeaxanthin epoxidase gene, also known as an aba-1 gene, is an abscisic acid (ABA) synthase that can catalyze oxidative conversion of the zeaxanthin into all-trans violaxanthin, thereby generating carotenoid precursors required in an ABA biosynthetic pathway. Furthermore, a core peptide segment that interacts with the aba1 is obtained by continuously reducing the length of a GSS1 sequence and conducting one-to-one yeast two-hybrid verification with the aba1 sequence.