The gene products of the ugp operon of Escherichia coli are responsible for the uptake of sn-glycerol-3-phosphate and certain glycerophosphodiesters. The regulation of ugp is mainly phoBR-dependent. Significant expression, however, can be observed even in the presence of high concentrations of phosp
Characterization of the ugp region containing the genes for the phoB dependent sn-glycerol-3-phosphate transport system of Escherichia coli
β Scribed by Schweizer, Herbert ;Boos, Winfried
- Publisher
- Springer
- Year
- 1984
- Tongue
- English
- Weight
- 850 KB
- Volume
- 197
- Category
- Article
- ISSN
- 0026-8925
No coin nor oath required. For personal study only.
β¦ Synopsis
The ugp structural genes, coding for the pho regulon dependent sn-glycerol-3-phosphate transport system, were cloned in pBR322 and characterized. The expression of the cloned ugp system was phoB dependent. Cells containing the ugp plasmid overproduced the G3P binding protein upon phosphate starvation. Tn5 mutagenesis of the cloned DNA revealed that the ugp genes are organized in two separate operons which comprise at least four genes: ugpB and ugpD constitute one operon, ugpA and ugpC constitute the other. The structural gene for the G3P binding protein (G3PBP) is ugpB. The ugpC gene product was also synthesized in minicells as a polypeptide, with an apparent molecular weight of 40,000. No gene products could be assigned to the ugpA and ugpD genes. Hybridization experiments allowed the physical characterization of 20 kb of DNA adjacent to the ugp genes on the E. coli chromosome including the liv genes.
π SIMILAR VOLUMES
## Abstract Two types of proteins are discussed in their role of facilitating the transport of maltose and __sn__βglycerolβ3βphosphate in __E. coli__. The first protein is the receptor for phage Ξ΄, known to be an outer membrane protein. By facilitating the diffusion of maltose and the higher maltod