中国少棘蜈蚣与家蚕和野桑蚕肌球蛋白轻链2的结构功能分析比较

Analysis and Comparison of Structure and Function of Myosin Light Chain 2 From Scolopendra subspinipes mutilans,Bombyx mori and Bombyx mandarina

从中国少棘蜈蚣(Scolopendra subspinipes mutilans)毒腺cDNA文库中克隆的肌球蛋白轻链2(MLC2)基因的cDNA,其开放阅读框为606 bp(GenBank登陆号为FJ262953),编码201个氨基酸,与家蚕(Bombyx mori)和野桑蚕(Bombyxmandarina)的MLC2等长,序列一致性达52%。3种MLC2都包含:1个同位且完整的EF-H功能域和Ca2+结合位,1个N端poly-lys基序及相同的丝氨酸磷酸化修饰位点。三级结构预测显示中国少棘蜈蚣MLC2的三维结构相似于乌贼(Loligo pealei)的同源模型,而家蚕和野桑蚕的则与淡色库蚊(Culexpipiens pallens)的MLC2一样类似于扇贝(Aequipecten irradians)的同源结构。分析结果有助于进一步研究家蚕和野桑蚕MLC2的结构功能及其功能应用。

The ORF of myosin light chain 2 （MLC 2） was cloned from venom gland cDNA library of Chinese centipede, Scolopendra subspinipes mutilans, which contains 606 nucleotides （GenBank accession number FJ262953） and encodes 201 amino acids. Bioinformatics analysis results showed that the length of MLC2 from Scolopendra subspinipes mutilans （SsmMLC2） is the same as that of MLC2 from Bombyx mori （BmMLC2） and Bombyx mandarina （BmmMLC2）. Sequence of SsmMLC2 has 52% identity with that of BmMLC2. Domains and active sites of SsmMLC2, BmMLC2, and BmmMLC2 are conserved, including the first complete EF-hand containing a calcium ion binding site, the N terminal poly-lys motif, and the phosphoserine phosphorylation site. Predicted 3D structure of SsmMLC2 is similar to the model of Loligo pealei MLC2, while BmMLC2, BmmMLC2 and Culex pipiens pallens MLC2 are similar to the model of Aequipecten irradians MLC2. The above results will provide favorable reference for further research on the relationship between structure and function of BmMLC2 and BmmMLC2.