The Streptomyces ATP-binding component MsiK assists in cellobiose and maltose transport
- 1 March 1997
- journal article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 179 (6) , 2092-2095
- https://doi.org/10.1128/jb.179.6.2092-2095.1997
Abstract
Streptomyces reticuli harbors an msiK gene which encodes a protein with an amino acid identify of 90% to a corresponding protein previously identified in Streptomyces lividans. Immunological studies revealed that S. lividans and S. reticuli synthesize their highest levels of MsiK during growth with cellobiose, but not with glucose. Moreover, moderate amounts of MsiK are produced by both species in the course of growth with maltose, melibiose, and xylose and by S. lividans in the presence of xylobiose and raffinose. In contrast, a recently identified cellobiose-binding protein and its distantly related homolog were only found if S. reticuli or S. lividans, respectively, was cultivated with cellobiose. Uptake of cellobiose and maltose was tested and ascertained for S. reticuli and S. lividans, but not for an msiK S. lividans mutant. However, transformants of this mutant carrying the S. reticuli or S. lividans msiK gene on a multicopy plasmid had regained the ability to transport both sugars. The data show that MsiK assists two ABC transport systems.Keywords
This publication has 29 references indexed in Scilit:
- A Lipid‐Anchored Binding Protein is a Component of an ATP‐Dependent Cellobiose/Cellotriose‐Transport System from the Cellulose Degrader Streptomyces reticuliEuropean Journal of Biochemistry, 1996
- A putative helical domain in the MalK subunit of the ATP‐binding‐cassette transport system for maltose of Salmonella typhimurium (MalFGK2) is crucial for interaction with MalF and MalG. A study using the LacK protein of Agrobacterium radiobacter as a tool.Molecular Microbiology, 1996
- A cellulase/xylanase-negative mutant of Streptomyces lividans 1326 defective in cellobiose and xylobiose uptake is mutated in a gene encoding a protein homologous to ATP-binding proteinsMolecular Microbiology, 1995
- Three Highly Homologous Membrane-bound Lipoproteins Participate in Oligopeptide Transport by the Ami System of the Gram-positive Streptococcus pneumoniaeJournal of Molecular Biology, 1994
- The gene encoding the cellulase (Avicelase) Cell from Streptomyces reticuli and analysis of protein domainsMolecular Microbiology, 1992
- ABC Transporters: From Microorganisms to ManAnnual Review of Cell Biology, 1992
- A Bacillus subtilis dipeptide transport system expressed early during sporulationMolecular Microbiology, 1991
- A chimeric nucleotide‐binding protein, encoded by a hisP–malK hybrid gene, is functional in maltose transport in Salmonella typhimuriumMolecular Microbiology, 1991
- Active Transport of Maltose in Escherichia coli K12European Journal of Biochemistry, 1974
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970