These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Extensive homology between membrane-associated components of histidine and maltose transport systems of Salmonella typhimurium and Escherichia coli.
    Author: Gilson E, Higgins CF, Hofnung M, Ferro-Luzzi Ames G, Nikaido H.
    Journal: J Biol Chem; 1982 Sep 10; 257(17):9915-8. PubMed ID: 7050111.
    Abstract:
    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.
    [Abstract] [Full Text] [Related] [New Search]