Cell-free synthesis of proteins related to sn-glycerol-3-phosphate transport in Escherichia coli.
AUTOR(ES)
Schumacher, G
RESUMO
An Escherichia coli periplasmic protein (GlpT) related to sn-glycerol-3-phosphate transport was synthesized in a cell-free system directed by hybrid plasmic ColE1-glpT DNA. The in vitro product cross-reacted with antisera against the purified protein. The ColE1-glpT DNA-directed cell-free system was induced by sn-glycerol-3-phosphate and phosphonomycin and was dependent on cyclic AMP. The in vitro-synthesized protein showed the characteristics of a multimeric protein, as did the purified periplasmic protein. The main proportion of the newly synthesized product had a higher molecular weight than the mature protein found in the periplasm of cells and showed a more positive charge in two-dimensional gel electrophoresis. Thus, a proportion of this protein is presumed to be synthesized in vitro as a precursor. The cell-free system yielded a second protein that is likely to be also coded for by the glpT operon. This protein had a molecular weight of approximately 33,000 in sodium dodecyl sulfate-acrylamide gel electrophoresis and behaved like an intrinsic membrane protein.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=224812Documentos Relacionados
- Periplasmic protein related to the sn-glycerol-3-phosphate transport system of Escherichia coli.
- A second transport system for sn-glycerol-3-phosphate in Escherichia coli.
- sn-Glycerol-3-phosphate transport in Salmonella typhimurium.
- Pi exchange mediated by the GlpT-dependent sn-glycerol-3-phosphate transport system in Escherichia coli.
- Structural characterization of ordered arrays of sn-glycerol-3-phosphate acyltransferase from Escherichia coli.