@article{199301,
  keywords = {Bacterial Proteins, Genes, Mutation, Escherichia coli, Escherichia coli Proteins, Cell Membrane, Carrier Proteins, ATP-Binding Cassette Transporters, beta-Galactosidase, Chromosomes, Bacterial, Genotype, Molecular Weight, Maltose, Maltose-Binding Proteins, Monosaccharide Transport Proteins},
  author = {Shuman and Silhavy},
  title = {Identification of the malK gene product. A peripheral membrane component of the Escherichia coli maltose transport system},
  abstract = {<p>The malK gene product of Escherichia coli has been identified through the use of a previously described technique that employs gene fusions (Shuman, H. A., Silhavy, T. J., and Beckwith, J. R. (1980) J. Biol. Chem. 255, 168-174). This protein, along with the four other products of the malB locus, comprise the complete maltose transport system. The malK protein has a molecular weight of approximately 40,000 and is located in the cell envelope. In mutant strains which lack another component of the transport system, the malG protein, the malK protein is located in the cytoplasm. This alteration in location suggests that the malK protein is associated with the inner surface of the cytoplasmic membrane via an interaction with the malG protein.</p>
},
  year = {1981},
  journal = {J Biol Chem},
  volume = {256},
  pages = {560-2},
  month = {01/1981},
  issn = {0021-9258},
  language = {eng},
}