刚毛柽柳RING型E3泛素连接酶基因的克隆及表达分析

IThe ubiquitin ligase E3 is a complex protein family that plays an important role not only in plant growth and development but also in response to various stresses. A full length cDNA of a RING-type E3 ubiquitin ligase(named ThE3) was isolated from the transcriptome cDNA librarys of Tamarix hispida. ThE3 was 2499 bp in length, including an open reading frame of 1275 bp which was predicted to encode a polypeptide of 424 amino acids. The estimated molecular weight and isoelectric points of the putatCloning and Expression Analysis of RING E3 ubiquitin - ligase Gene from Tamarix hispidaive protein were 45.8 kD and 8.30, respectively. Hydrophobic analysis predicts that RING type E3 ubiquitin ligase has strong hydrophilicity, no signal peptide and transmembrane region, and subcellular localization on the nucleus.Amino acid sequence analysis shows that ThE3 show 76% similarities in amino acid sequence to homology from Nelumbo nucifera. And the RING-finger domain was used to determine the ThE3 as the RING-finger type E3 ubiquitin ligase gene of Tamarix hispida. Quantitative real-time PCR assay revealed that the mRNA levels of ThE3 was significantly up-regulated under NaCl and PEG treatments in Tamarix hispida, suggesting that ThE3 might play an improtant role in salt and drought tolerance of Tamarix hispida.