Extensive homology between membrane-associated components of histidine and maltose transport systems of Salmonella typhimurium and Escherichia coli.

Extensive homology between membrane-associated components of histidine and maltose transport systems of Salmonella typhimurium and Escherichia coli.
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DOI:
10.1016/s0021-9258(18)33962-0
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发表时间:
1982-09
期刊:
The Journal of biological chemistry
影响因子:
--
通讯作者:
E. Gilson;C. Higgins;M. Hofnung;G. Ames;H. Nikaido
E. Gilson;C. Higgins;M. Hofnung;G. Ames;H. Nikaido
中科院分区:
其他
文献类型:
--
作者:
E. Gilson;C. Higgins;M. Hofnung;G. Ames;H. Nikaido

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鼠伤寒沙门氏菌高亲和力组氨酸转运系统(由 hisP 基因编码)和大肠杆菌麦芽糖-麦芽糖糊精转运系统(由 malK 基因编码)的细胞质膜相关成分的氨基酸序列(从 DNA 核苷酸序列推导)之间发现了很强的同源性。当HisP蛋白序列与MalK蛋白NH2末端三分之二的序列比对时,32%的位置是相同的,另外35%的位置被功能相似的氨基酸残基占据。这些结果表明,一些(可能是许多)“周质结合蛋白依赖性”运输系统是从共同的祖先系统进化而来的。
A strong homology was found between the amino acid sequences, deduced from DNA nucleotide sequences, of cytoplasmic membrane-associated components of the high affinity histidine transport system of Salmonella typhimurium (coded by the hisP gene) and the maltose-maltodextrin transport system of Escherichia coli (coded by the malK gene). When the HisP protein sequence was aligned with that of the NH2-terminal two-thirds of the MalK protein, 32% of the positions were identical, and an additional 35% were occupied by functionally similar amino acid residues. These results suggest that some, and possibly many, "periplasmic-binding protein-dependent" transport systems have evolved from a common ancestral system.