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透明质酸合酶:来自链霉菌属菌株的基因克隆与测序

Hyaluronate synthase: cloning and sequencing of the gene from Streptococcus sp.

作者信息

Lansing M, Lellig S, Mausolf A, Martini I, Crescenzi F, O'Regan M, Prehm P

机构信息

Institut für Physiologische Chemie und Pathobiochemie, Münster, Federal Republic of Germany.

出版信息

Biochem J. 1993 Jan 1;289 ( Pt 1)(Pt 1):179-84. doi: 10.1042/bj2890179.

Abstract

The complete nucleotide sequence of hyaluronate synthase from Streptococcus sp. and its flanking regions is presented. The gene locus was designated has. Southern-blotting results suggested that the gene was conserved in hyaluronate-producing streptococci. A putative translation-initiation codon was identified and the open reading frame consists of 1566 bp, specifying a protein of 56 kDa. Sequences resembling the promoter and ribosome-binding site of Gram-positive organisms are found upstream of the synthase. The predicted amino-acid sequence reveals the presence of a 35-residue signal peptide. The sequence has some similarity to bacterial peptide-binding proteins.

摘要

本文展示了来自链球菌属的透明质酸合酶及其侧翼区域的完整核苷酸序列。该基因位点被命名为has。Southern印迹结果表明该基因在产生透明质酸的链球菌中是保守的。确定了一个推定的翻译起始密码子,开放阅读框由1566 bp组成,编码一个56 kDa的蛋白质。在合酶上游发现了类似于革兰氏阳性菌启动子和核糖体结合位点的序列。预测的氨基酸序列显示存在一个35个残基的信号肽。该序列与细菌肽结合蛋白有一定的相似性。

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