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:
影响因子:
--
通讯作者:
E. Gilson;C. Higgins;M. Hofnung;G. Ames;H. Nikaido
中科院分区:
文献类型:
--
作者:
E. Gilson;C. Higgins;M. Hofnung;G. Ames;H. Nikaido
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.