Cytoplasmic membrane active transport system

In microbes without a permeability barrier, or when the barrier fails, a mechanism must be in place to export metals from the cytoplasm. These active transport systems involve energy-dependent, membrane-bound efflux pumps that can be encoded by either chromosomal- or plasmid-borne genes. Active transport is the most well-studied metal resistance mechanism. Some of these include the ars operon for exporting arsenic from E. coli, the cad system for exporting cadmium from Staphylococcus aureus, and the cop operon for removing excess copper from Enterococcus hiraeP i9A0... 

Biochemically, most quaternary ammonium compounds function as receptor-specific mediators. Because of their hydrophilic nature, small molecule quaternaries caimot penetrate the alkyl region of bdayer membranes and must activate receptors located at the cell surface. Quaternary ammonium compounds also function biochemically as messengers, which are generated at the inner surface of a plasma membrane or in a cytoplasm in response to a signal. They may also be transferred through the membrane by an active transport system. 

The situation may be different with microorganisms, although here, too, secondary active transport of nutrients and metabolites appears to be firmly established for many transport systems. Especially the membrane bound (shock-resistant) systems which appear to be firmly incorporated in the cytoplasmic membrane are rather clearly identified as secondary active transport systems, as they require an energized state of the membrane, which means that they are driven by a proton-motive force, i.e. an electrochemical potential gradient of H -ions [3]. 

In the hyphal cells of P. cyclopium two pools exist for L-phenylalanine a low capacity, peripheral p6ol (the cytoplasm), and a central , expandable pool (the vacuoles) (Fig. 9). L-Phenylalanine is transported by several carrier systems through the plasma membrane and by an active transport system through the vacuole membrane. 

The transport of must hexose (glucose and fructose) across the plasmic membrane activates a complex system of proteinic transporters not fully explained (Section 1.3.2). This mechanism facilitates the diffusion of must hexoses in the cytoplasm, where they are rapidly metabolized. Since solute moves in the direction of the concentration gradient, from the concentrated outer medium to the diluted inner medium, it is not an active transport system requiring energy. 

Figure 3. Hierarchical levels of metabolic control. Sites of metabolic control are designated as (1) plasma membrane level active transport systems, hormone receptors (2) cytoplasmic level hormone binding protein complex, signal molecule generation (3) enzymatic level steady-state enzymatic pathway, servomechanisms, enzyme degradation (4) ribosomal level protein biosynthesis (5) nuclear level hormonal control of gene action, operon control of gene action (substrate induction, product repression). The symbol,, indicates inhibition of a reaction.

Likewise, for zinc, bacteria have developed active uptake systems (Hantke, 2001). In many bacteria the high-affinity Zn2+ uptake system uses an ABC transporter of the cluster 9 family, which mostly transports zinc and manganese and is found in nearly all bacterial species. First identified in cyanobacteria and pathogenic streptococci, but also found in E. coli, the system is encoded by three genes ZnuABC and consists of an outer membrane permease ZnuB, a periplasmic-binding protein ZnuA and a cytoplasmic ATPase ZnuC. Low-affinity transporters of the ZIP family, described later in this chapter, such as ZupT, have also been shown to be involved in bacterial zinc uptake. 

The inner mitochondrial membrane has a group-specific transport system for fatty acids. In the cytoplasm, the acyl groups of activated fatty acids are transferred to carnitine by carnitine acyltransferase [1 ]. They are then channeled into the matrix by an acylcar-nitine/carnitine antiport as acyl carnitine, in exchange for free carnitine. In the matrix, the mitochondrial enzyme carnitine acyltransferase catalyzes the return transfer of the acyl residue to CoA. 

Although all tetracyclines have a similar mechanism of action, they have different chemical structures and are produced by different species of Streptomyces. In addition, structural analogues of these compounds have been synthesized to improve pharmacokinetic properties and antimicrobial activity. While several biological processes in the bacterial cells are modified by the tetracyclines, their primary mode of action is inhibition of protein synthesis. Tetracyclines bind to the SOS ribosome and thereby prevent the binding of aminoacyl transfer RNA (tRNA) to the A site (acceptor site) on the 50S ri-bosomal unit. The tetracyclines affect both eukaryotic and prokaryotic cells but are selectively toxic for bacteria, because they readily penetrate microbial membranes and accumulate in the cytoplasm through an energy-dependent tetracycline transport system that is absent from mammalian cells. 

The most universal transport systems are those involved in the transport of the ubiquitous inorganic ions, sodium, potassium and calcium1. The sodium pump counteracts passive water movement across the cell membrane by removing sodium ions together with chloride or other anions from the cytoplasm to lower its content of osmotically active substances. In most cells, however, the elimination of sodium ions is connected with an accumulation of potassium ions6. For three sodium ions leaving the cell two potassium ions are taken up9,10). The resulting concentration... 

---