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Abstract
In Brassica napus , ATP6 is related to Pol cytoplasmic male sterility. To understand the mechanism of Pol CMS, proteins which interact with ATP6 were screened in a yeast two-hybrid system. A partial sequence of a putative and ascorbate peroxidase ( Bn-APX ) was isolated from Brassica napus . By use of rapid amplification of cDNA ends method, the full length of Bn-APX coding sequence was cloned. The deduced amino acid sequence contained 438 amino acid residues with a conserved ascorbate peroxidase domain and shared 77% identity with that of APX from Arabidopsis thaliana . Further analyses revealed that the region of Bn-APX interacting with ATP6 was at its c-terminal. It was also observed that the expressions of ATP6 and Bn-APX were strongly similar in the floral tissue of CMS line and the restoring line. Furthermore, in restoring line, the expression of Bn-APX is higher in the flower than that in other tissues.
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