G. Merino et Ha. Shuman, TRUNCATION OF MALF RESULTS IN LACTOSE TRANSPORT VIA THE MALTOSE TRANSPORT-SYSTEM OF ESCHERICHIA-COLI, The Journal of biological chemistry, 273(4), 1998, pp. 2435-2444
The active accumulation of maltose and maltodextrins by Escherichia co
li is dependent on the maltose transport system. Several lines of evid
ence suggest that the substrate specificity of the system is not only
determined by the periplasmic maltose-binding protein but that a furth
er level of substrate specificity is contributed by the inner membrane
integral membrane components of the system, MalF and MalG. We have is
olated and characterized an altered substrate specificity mutant that
transports lactose. The mutation responsible for the altered substrate
specificity results in an amber stop codon at position 99 of MalF. Th
e mutant requires functional MalK-ATPase activity and hydrolyzes ATP c
onstitutively. It also requires MalG. The data suggest that in this mu
tant the MalG protein is capable of forming a low affinity transport p
ath for substrate.