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Small GTP-binding proteins function as regulators of specific intercellular fundamental biological processes. In this study, a small GTP-binding protein Rab7 gene, designated as  TaRab7 , was identified and characterized from a cDNA library of wheat leaves infected with  Puccinia striiformis  f. sp.  tritici  ( Pst ) the wheat stripe rust pathogen. The gene was predicted to encode a protein of 206 amino acids, with a molecular mass of 23.13 KDa and an isoeletric point (pI) of 5.13. Further analysis revealed the presence of a conserved signature that is characteristic of Rab7, and phylogenetic analysis demonstrated that TaRab7 has the highest similarity to a small GTP binding protein gene (BdRab7-like) from  Brachypodium distachyon . Quantitative real-time PCR assays revealed that the expression of  TaRab7  was higher in the early stage of the incompatible interactions between wheat and  Pst  than in the compatible interaction, and the transcription level of  TaRab7  was also highly induced by environmental stress stimuli. Furthermore, knocking down  TaRab7  expression by virus induced gene silencing enhanced the susceptibility of wheat cv. Suwon 11 to an avirulent race CYR23. These results imply that  TaRab7  plays an important role in the early stage of wheat-stripe rust fungus interaction and in stress tolerance.

Wheat TaRab7 GTPase Is Part of the Signaling Pathway in Responses to Stripe Rust and Abiotic Stimuli