Banas J A, Simon D, Williams L K, Ferretti J J, Russell R R
Department of Microbiology, University of Oklahoma H.S.C., Oklahoma City 73190.
FEMS Microbiol Lett. 1994 Nov 1;123(3):349-54. doi: 10.1111/j.1574-6968.1994.tb07247.x.
A glucosyltransferase (GTF) gene, designated gtfL, from Streptococcus salivarius was cloned and expressed in Escherichia coli and its nucleotide sequence determined. The GTF-L enzyme catalysed the synthesis of water-insoluble glucan in a primer-independent manner. The nucleotide sequence and derived amino acid sequence of GTF-L were similar in size and domain structure to previously sequenced glucosyltransferases. However, a 464-bp region of high variability was identified which could be selectively amplified from strains of S. salivarius by the polymerase chain reaction and could therefore form the basis for species identification. No sequence-specific motifs related to the solubility and linkage of the glucan product or its need for a dextran primer could be ascertained.
从唾液链球菌中克隆出一个名为gtfL的葡糖基转移酶（GTF）基因，并在大肠杆菌中进行表达，同时测定了其核苷酸序列。GTF-L酶以不依赖引物的方式催化水不溶性葡聚糖的合成。GTF-L的核苷酸序列和推导的氨基酸序列在大小和结构域结构上与先前测序的葡糖基转移酶相似。然而，鉴定出一个464bp的高变区，该区域可通过聚合酶链反应从唾液链球菌菌株中选择性扩增，因此可作为物种鉴定的基础。未发现与葡聚糖产物的溶解性和连接或其对葡聚糖引物的需求相关的序列特异性基序。
