Olsson A, Eliasson M, Guss B, Nilsson B, Hellman U, Lindberg M, Uhlén M
Department of Biochemistry, Royal Institute of Technology, Stockholm, Sweden.
Eur J Biochem. 1987 Oct 15;168(2):319-24. doi: 10.1111/j.1432-1033.1987.tb13423.x.
The complete sequence of the structural gene encoding the immunoglobulin G binding protein from Streptococcus G148 has been determined, as well as its 5' and 3' flanking sequences. The sequence reveals an open reading frame encoding a putative preprotein with a relative molecular mass of 63294. N-Terminal sequencing of the mature protein, spontaneously released from streptococcal cells, demonstrates that the signal peptide consists of 33 amino acids. The DNA sequence reveals extensive internal homologies similar to other cell-wall-bound receptors from gram-positive bacteria. Comparisons with a related gene previously isolated from another strain of streptococci revealed large differences in size, due to variations in the number of internal repeats. The structure of the gene suggests an evolution through multiple duplications.
已确定来自链球菌G148的编码免疫球蛋白G结合蛋白的结构基因的完整序列及其5'和3'侧翼序列。该序列揭示了一个开放阅读框，编码一个相对分子质量为63294的假定前体蛋白。从链球菌细胞中自发释放的成熟蛋白的N端测序表明，信号肽由33个氨基酸组成。DNA序列显示出与革兰氏阳性菌其他细胞壁结合受体相似的广泛内部同源性。与先前从另一株链球菌中分离出的相关基因进行比较，发现由于内部重复序列数量的变化，大小存在很大差异。该基因的结构表明其通过多次重复进化而来。
