A. Schlosser et al., TRKH AND ITS HOMOLOG, TRKG, DETERMINE THE SPECIFICITY AND KINETICS OFCATION-TRANSPORT BY THE TRK SYSTEM OF ESCHERICHIA-COLI, Journal of bacteriology, 177(7), 1995, pp. 1908-1910
The corrected sequence of the trkH gene of Escherichia coli predicts t
hat the TrkH protein is a hydrophobic membrane protein of 483 amino ac
id residues, of which 41% are identical to those of the homologous and
functionally analogous TrkG protein. These two proteins form the tran
smembrane component of the Trk system for the uptake of K+. Each prote
in alone is sufficient for high-level Trk activity. When Trk is assemb
led with the TrkG protein, Rb+ and K+ are transported with a K-m near
or below 1 mM; however, the V-max for Rb+ is only about 7% of that for
K+. When Trk is formed with TrkH, the affinities for both for K+ and
Rb+ are somewhat lower, and the V-max for Rb+ is only 1% of that for K
+ transport. The kinetics of transport in strains with wild-type allel
es at trkG and at trkH suggest that both products participate in trans
port.