烟草泛素激活酶E1氨基酸序列的分析

Analysis of Amino Acid Sequence of Tobacco Ubiquitin Activating Enzyme E1

泛素激活酶E1是促使泛素与蛋白质结合途径中的重要酶,为此,运用PROTPARAM、NetPhos和protscale工具分析烟草泛素激活酶E1成员的生理特性、磷酸化位点和疏水性。结果显示,NtUAE1、NtUAE2和NtUAE3属于稳定性蛋白,且耐热性较强,半衰期均大于20 h,均属于酸性氨基酸,三者各序列中的氨基酸含量占比位于为Pro、Asp和Leu;NtUAE1、NtUAE2和NtUAE3的磷酸化位点分别为83、77和75个,其中酪氨酸数目相同,均为7个;泛素激活酶E1成员均属于亲水性蛋白。

The ubiquitin-activating enzyme E1 is an important enzyme in the binding of ubiquitin to proteins. To this end, the physiological properties, phosphorylation sites and hydrophobicity of tobacco ubiquitin-activating enzyme E1 members were analyzed using PROTPARAM, NetPhos and protscale tools. The results showed that NtUAE1, NtUAE2 and NtUAE3 were stable proteins with high heat tolerance and half-life of more than 20 h, all of which belonged to acidic amino acids. The amino acid content of each of the three sequences was Pro, Asp and Leu;NtUAE1 The phosphorylation sites of NtUAE2 and NtUAE3 were 83, 77 and 75, respectively, and the number of tyrosines was the same, all of which were 7;the ubiquitin-activating enzyme E1 members were all hydrophilic proteins.