Escherichia coli, membrane proteins

Busse H-J, Wostmann C, Bakker EP The bactericidal action of streptomycin Membrane permeabilization caused by the insertion of mistranslated proteins into the cytoplasmic membrane of Escherichia coli and subsequent caging of the antibiotic inside the cells due to degradation of these proteins. J Gen Microbiol 1992 138 551. [PMID 1375623]... 

Ruiz, N., Cronenberg, L.S., Kahne, D., Silhavy, TJ. Identification of two inner-membrane proteins required for the transport of lipopolysaccharide to the outer membrane of Escherichia coli. Proc Natl Acad Sci USA 105 (2008) 5537-5542. 

Sperandeo, P., Lau, F.K., Carpentieri, A., De Castro, C., Molinaro, A., Deho, G., Silhavy, T.J., Polissi, A. Functional analysis of the protein machinery required for transport of lipopolysac-charide to the outer membrane of Escherichia coli. J Bacteriol 190 (2008) 4460 1469. 

The removal of the signal sequence which directs the transport of secreted proteins is a critical step in protein export. Extensive studies by Randall, Hardy and coworkers have demonstrated that the leader sequence prevents the proper folding of the mature polypeptide within the cytoplasm (55,54). For the E.coli 6-lactamase, the presence of the leader sequence decelerates the folding kinetics but does not prevent the formation of the enzymatically active conformation (55). Bowden and Georgiou (56) showed that the mode of translocation of 6-lactamase across the cytoplasmic membrane of Escherichia coli exerts a profound effect on the folding of the mature protein following secretion, presumably by affecting the unfolded state in the periplasmic space. 

Rutz, C., Rosenthal, W. and Schulein, R., A single negatively charged residue affects the orientation of a membrane protein in the inner membrane of Escherichia coli only when it is located adjacent to a transmembrane domain, J Biol Chem 274 (1999) 33757-33763. 

K. Ohyama, N. Hatanaka, S. Asahi et al. (2002). Roles of NADPH-P450 reductase and apo- and holo-cytochrome b5 on xenobiotic oxidations catalyzed by 12 recombinant human cytochrome P450s expressed in membranes of Escherichia coli. Protein Expr. Purif. 24, 329-337. 

Heller, K.B., 1978, Apparent molecular weights of a heat modifiable protein fi om the outer membrane of Escherichia coli in gels with different acrylamide concentrations. J. Bacterial. 134 1181-1183. 

Huang, R. and Reusch, R. N. Poly(3-hydroxybutyrate) is associated with specific proteins in the cytoplasm and membranes of Escherichia coli. J. Biol Chem. 1996, 271, 22196-22201. 

Huang R, Reusch RN (1996) Poly(3-hydroxybutyrate) Is Associated with Specific Proteins in the Cytoplasm and Membranes of Escherichia coli.22196— 22202. 

Garavito, R. M., et al., 1983. X-ray diffraction analysis of matrix porin, an integral membrane protein from Escherichia coli outer membrane. Journal of Nlolecular Biology 164 313—327. 

From a genetical point of view, Saccharomyces cerevisiae is an ideal organism which may be considered the Escherichia coli of eukaryotic cells [4,5]. This is true in particular for the study of metabolic regulation and for that of membrane transport [6]. Finally, the astonishing resemblance between many yeast proteins and certain mammalian-cell proteins has seriously broadened the scope of interest. Although a few reports have appeared on amino acid transport in some other yeasts, most investigations in this field have used strains of Saccharomyces cerevisiae. 

In bacteria, accumulation of substrates against a concentration gradient can occur through two main classes of transport systems (see [30] for a summary). The prototype of the first class of transporters is the /3-galactoside permease of Escherichia coli (see [31]). It is a relatively simple system involving only a single membrane-bound protein. It catalyzes a lactose-H symport. Other transporters... 

Derouiche, R., Benedetti, H., Lazzaroni, J.C., Lazdunski, C., and Lloubes, R. (1995) Protein complex within Escherichia coli inner membrane. TolA N-terminal domain interacts with TolQ and TolR proteins./. Biol. Chem. 270, 11078-11084. 

MIROUX, B., WALKER, J.E., Over-production of proteins in Escherichia coli Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels, J. Mol. Biol. 1996, 260, 289-298. 

Jung, K., Voss, J., He, M., Hubbell, W. L., and Kaback, H. R. (1995) Engineering a metal binding site within a polytopic membrane protein, the lactose permease of Escherichia coli. Biochemistry 34, 6272-6277. 

---