Synthesis of the Streptomyces lividans maltodextrin ABC transporter depends on the presence of the regulator MalR

FEMS Microbiol Lett. 2001 Mar 1;196(1):77-83. doi: 10.1111/j.1574-6968.2001.tb10544.x.

Abstract

During growth with maltotriose or amylose, Streptomyces lividans and Streptomyces coelicolor A3(2) synthesize a maltodextrin uptake system with highest specificity for maltotriose. The transport activity is absent in mutants of S. coelicolor A3(2) lacking a functional MalE binding protein. Cloning and sequencing data suggest that the mal operon of S. coelicolor A3(2) corresponds to the one of S. lividans and that the deduced S. lividans Reg1 amino acid sequence is identical to that of MalR from S. coelicolor A3(2). It can be concluded that both strains have the same ABC transport system for maltodextrins. The S. lividans malR was cloned in Escherichia coli in frame with six histidine-encoding codons. The resulting, purified 6HisMalR(SI) was shown to bind to two motifs within the S. lividans malR-malE intergenic region and to dissociate in the presence of maltopentaose.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ATP-Binding Cassette Transporters / biosynthesis*
  • Bacterial Proteins*
  • Binding Sites
  • Biological Transport
  • Cloning, Molecular
  • Maltose / metabolism
  • Molecular Sequence Data
  • Oligosaccharides / metabolism
  • Operator Regions, Genetic
  • Operon
  • Polysaccharides / metabolism*
  • Repressor Proteins / genetics*
  • Repressor Proteins / metabolism*
  • Streptomyces / genetics
  • Streptomyces / growth & development
  • Streptomyces / metabolism*
  • Trisaccharides / metabolism

Substances

  • ATP-Binding Cassette Transporters
  • Bacterial Proteins
  • Oligosaccharides
  • Polysaccharides
  • Repressor Proteins
  • Trisaccharides
  • malR protein, bacteria
  • maltopentaose
  • maltotriose
  • Maltose
  • maltodextrin

Associated data

  • GENBANK/AJ272397