变形链球菌scrB基因的序列分析
Sequence analysis of the Streptococcus mutans scrB gene.
作者信息
Sato Y, Kuramitsu H K
机构信息
Department of Microbiology-Immunology, Northwestern University Medical-Dental Schools, Chicago, Illinois 60611.
出版信息
Infect Immun. 1988 Aug;56(8):1956-60. doi: 10.1128/iai.56.8.1956-1960.1988.
Abstract
The complete nucleotide sequence of the Streptococcus mutans GS-5 scrB gene coding for sucrose-6-phosphate hydrolase activity was determined. A potential ribosome-binding site as well as promoter sequences were identified upstream from the gene. The deduced amino acid sequence of the enzyme suggested a molecular weight of 51,750, which is similar to that estimated for the enzyme isolated from strain GS-5. The enzyme is slightly acidic, with a pI of 5.9, and is a relatively hydrophilic protein. The nucleotide and amino acid sequences of the enzyme showed significant homology with those of the sacA protein from Bacillus subtilis. In addition, a region of amino acid homology with the S. mutans fructosyltransferase and B. subtilis levansucrase proteins was also detected.
摘要
测定了变形链球菌GS-5编码蔗糖-6-磷酸水解酶活性的scrB基因的完整核苷酸序列。在该基因上游鉴定出一个潜在的核糖体结合位点以及启动子序列。该酶推导的氨基酸序列表明其分子量为51,750，这与从GS-5菌株分离出的酶的估计分子量相似。该酶呈弱酸性，pI为5.9，是一种相对亲水的蛋白质。该酶的核苷酸和氨基酸序列与枯草芽孢杆菌的sacA蛋白的序列具有显著同源性。此外，还检测到与变形链球菌果糖基转移酶和枯草芽孢杆菌果聚糖蔗糖酶蛋白的氨基酸同源区域。
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