NUCLEOTIDE-SEQUENCE OF THE STREPTOCOCCUS MUTANS GTFD GENE ENCODING THE GLUCOSYLTRANSFERASE-S ENZYME

NUCLEOTIDE-SEQUENCE OF THE STREPTOCOCCUS MUTANS GTFD GENE ENCODING THE GLUCOSYLTRANSFERASE-S ENZYME
复制标题

DOI:
10.1099/00221287-136-10-2099
复制
发表时间:
1990-10-01
期刊:
JOURNAL OF GENERAL MICROBIOLOGY
影响因子:
--
通讯作者:
KURAMITSU, HK
KURAMITSU, HK
中科院分区:
其他
文献类型:
--
作者:
HONDA, O;KATO, C;KURAMITSU, HK

文献摘要

被引文献

相似文献

已确定编码合成水溶性葡聚糖(GTF-S)的葡糖基转移酶的变异链球菌GS-5 gtD基因的核苷酸序列。该基因全长4293个碱基,未加工蛋白由1430个氨基酸组成,分子量为159814 Da,其氨基端与其它胞外蛋白的信号肽序列相似。变形链球菌和唐内链球菌分泌的GTF-1的表达。此外,GTF-S蛋白与本实验室先前分离和测序的负责不溶性葡聚糖合成的菌株GS-5酶(GTF-I,GTF-SI)具有高度的氨基酸相似性。这些结果表明,所有三个gtf基因进化自一个共同的祖先基因。
The nucleotide sequence of the Streptococcus mutans GS-5 gtD gene coding for the glucosyltransferase which synthesizes water-soluble glucan (GTF-S) has been determined. The complete gene contains 4293 base pairs and the unprocessed protein is composed of 1430 amino acids with a molecular mass of 159814 Da. The amino terminus of the unprocessed protein resembles the signal sequences of other extracellular proteins secreted by S. mutans and that of the GTF-I secreted by Streptococcus downei. In addition, the GTF-S protein exhibits high amino acid similarity with the strain GS-5 enzymes responsible for insoluble glucan synthesis (GTF-I, GTF-SI) previously isolated and sequenced in this laboratory. These results indicate that all three gtf genes evolved from a common ancestral gene.