IDENTIFICATION OF A PUTP PROLINE PERMEASE GENE HOMOLOG FROM STAPHYLOCOCCUS-AUREUS BY EXPRESSION CLONING OF THE HIGH-AFFINITY PROLINE TRANSPORT-SYSTEM IN ESCHERICHIA-COLI
Pa. Wengender et Kj. Miller, IDENTIFICATION OF A PUTP PROLINE PERMEASE GENE HOMOLOG FROM STAPHYLOCOCCUS-AUREUS BY EXPRESSION CLONING OF THE HIGH-AFFINITY PROLINE TRANSPORT-SYSTEM IN ESCHERICHIA-COLI, Applied and environmental microbiology, 61(1), 1995, pp. 252-259
The important food-borne pathogen Staphylococcus aureus is distinguish
ed by its ability to grow at low water activity values. Previous work
in our laboratory and by others has revealed that proline accumulation
via transport is an important osmoregulatory strategy employed by thi
s bacterium, Furthermore, proline uptake by this bacterium has been sh
own to be mediated by two distinct transport systems: a high-affinity
system and a low-affinity system (J.-H. Bae, and K. J. Miller, Appl. E
nviron. Microbiol. 58:471-475, 1992; D. E. Townsend and B. J. Wilkinso
n, J. Bacteriol. 174:2702-2710, 1992). In the present study, we report
the cloning of the high-affinity proline transport system of S. aureu
s by functional expression in an Escherichia coli host. The sequence o
f the staphylococcal proline permease gene was predicted to encode a p
rotein of 497 amino acids which shares 49% identity with the PutP high
-affinity proline permease of E. coli. Analysis of hydropathy also ind
icated a common overall structure for these proteins.