文摘
Protein modification by ubiquitin (Ub) and ubiquitin-like proteins (Ubls) is among the most complex and heavily investigated mechanisms of posttranslational protein regulation in eukaryotes. Moreover, Ub plays diverse roles in the regulation of numerous biological pathways. In this study, a suppression-subtractive hybridization cDNA library has been constructed using RNA isolated from leaves of the wheat line SN6306 inoculated with Blumeria graminis as the tester and RNA from non-inoculated leaves as the driver. Eighteen expressed sequence tags (ESTs) highly homologous with known proteins involved in disease resistance and defense reactions have been identified. Among these, a 648?bp EST with a high degree of sequence similarity in both nucleic and amino acid levels to other members of the gene family of plant related-to-ubiquitin (RUB) proteins has been selected, and its genomic sequence obtained. The cDNA sequence of this EST is interrupted by two introns at 111 and 1450?bp, with an open reading frame of 462?bp that encodes 153 amino acids. The predicated protein is a fusion protein of an ubiquitin-coding region and an RUB region. The newly screened gene, designated as TaRUB1 (GenBank Accession No. JF927719) belongs to the family of wheat RUB genes. Quantitative real-time polymerase chain reaction revealed that TaRUB1 is upregulated in leaves infected with powdery mildew during early stages of infection. Furthermore, the overexpression of TaRUB1 in transgenic Arabidopsis showed that TaRUB1 enhances plant tolerance to both osmotic and salt stresses. This finding suggests that TaRUB1 has multiple functions in plant abiotic and biotic stress tolerance.