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作 者:孟利强[1,2] 沙长青[1,3] 张先成[1] 张淑梅[1,2] 赵晓宇[1,2] 曹旭[1,2] 李晶[1,2]
机构地区:[1]黑龙江省科学院微生物研究所生物工程重点实验室,黑龙江哈尔滨150010 [2]黑龙江省科学院高技术研究院,黑龙江哈尔滨150020 [3]黑龙江省科学院条件财务处,黑龙江哈尔滨150001
出 处:《微生物学杂志》2016年第1期62-68,共7页Journal of Microbiology
基 金:黑龙江省科学院学科团队创新能力提升专项(2014ws09)
摘 要:通过生物信息学技术对Chi A基因序列进行分析预测,了解Chi A的基因结构及蛋白质性质。从自有菌株(粘质沙雷氏菌Serratia mareescens S68)中克隆到几丁质酶基因Chi A,利用相关软件对Chi A基因序列进行分析预测。Chi A基因全长1 714 bp,开放阅读框编码563个氨基酸,推测其编码的蛋白质分子量为60 983.8Da,等电点为6.35,是一种稳定的亲水性蛋白质。预测Chi A可能存在信号肽,切割位点在第23~24位氨基酸之间,1~23位氨基酸为其跨膜结构,其余肽链位于细胞外。Chi A主要存在3种二级结构元件,在二级、三级结构中都有体现。该Chi A是一种水溶性蛋白质,结构稳定且可以分泌到胞外。In order to learn the structure of chitinase gene( Chi A) and the protein properties of Chi A,the sequence of Chi A was analyzed and predicted by bioinformatics techniques. Chi A was cloned from Serratia marcescens strain41003,its sequence was analyzed and predicted by bioinformatics software. The results showed that the length of Chi A was 1 714 bp having an open reading frame encoding 563 amino acids inferring their encoded protein molecular weight at 60 983. 8 Da with isoelectric point at 6. 35,it was a stable hydrophilic protein. It was predicted that it might exist a signal peptide in Chi A with its cutting site between 23 rd to 24 th amino acid. 1st to 23 rd amino acid might be the transmembrane construction and the rest peptide chains located outside the cell. Chi A mainly existed three kinds of secondary structure elements,which embodied in both secondary structure and tertiary structure. Therefore,Chi A was a hydrosoluble protein with stable structure and could be secreted outside the cell.
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