Gram-negative bacteria proteins

Streptomycin Streptomyces griseus Gram-negative bacteria Protein synthesis... 

Nakai, K., and Kanehisa, M. (1991). PROTEINS Structure, function, and genetics expert system for predicting protein localization sites in gram-negative bacteria. Proteins Struct. Fund. Genet. 11, 95-110. 

Guo, J., Lin, Y, Liu, X. GNBSL A new integrative system to predict the subceUular location for gram-negative bacteria proteins. Proteomics 2006, 6,5099-105. 

Gram-negative bacteria are surrounded by two membranes, an inner plasma membrane and an outer membrane. These are separated by a periplasmic space. Most plasma membrane proteins contain long, continuous sequences of about 20 hydrophobic residues that are typical of transmembrane a helices such as those found in bacteriorhodopsin. In contrast, most outer membrane proteins do not show such sequence patterns. 

Currently, five different molecular classes of mdr efflux pumps are known [5], While pumps of the the ATP-binding cassette (ABC) transporter superfamily are driven by ATP hydrolysis, the other four superfamilies called resistance-nodulation-division (RND), major facilitator superfamily (MFS), multidrug and toxic compound extrusion (MATE), and small multidrag resistance transporter (SMR) are driven by the proton-motive force across the cytoplasmic membrane. Usually a single pump protein is located within the cytoplasmic membrane. However, the RND-type pumps which are restricted to Gram-negative bacteria consist of two additional components, a periplasmic membrane fusion protein (MFP) which connects the efflux pump to an outer... 

The surface structure of gram-negative bacteria (these are not stained by Gram s method and must be stained red with carbol fuchsin) is more diversified. It consists of an outer membrane whose main building unit is a lipopolysaccharide together with phospholipids and proteins. The actual cell... 

The high space-time yields are the result of a doubling time of only 30 min and its applicability for high cell-density cultures. However, it is hardly possible to excrete overexpressed proteins into cultivation media. In addition, accumulation of pyrogenic lipopoly-saccharides in its outer membrane (a distinctive feature of Gram-negative bacteria) make additional purification steps necessary if pharmaceutical proteins are produced by E. coli [29]. 

E. coli, like other Gram-negative bacteria, has an outer membrane which hampers excretion of proteins to the culture media. Thus, expressed proteins can remain in the cytoplasm or can be directed into the periplasm employing the N-terminus fusion of a signal peptide (e.g. OmpA, pelB, OmpF, PhoA, Tat signal peptides) [30]. 

The Fur protein regulates iron uptake systems in many Gram-negative bacteria. The striking phenotype of the first fur mutants isolated was the overexpression of the outer membrane receptors for siderophore iron transport. In addition, excretion of siderophores under iron-rich growth conditions was observed in these mutants, indicating that the biosynthesis of siderophores is also regulated by Fur. 

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