Disease relevance of traH

• Lipoprotein PssN of Rhizobium leguminosarum bv. trifolii: Subcellular Localization and Possible Involvement in Exopolysaccharide Export [1].
• We have constructed a tripartite fusion consisting of (i) the signal sequence and first nine N-terminal amino acids of the mature major Escherichia coli lipoprotein, (ii) amino acids 46-159 of the outer membrane protein OmpA, and (iii) the complete mature beta-lactamase (EC 3.5.2.6) sequence [2].
• A human anti-CD22 single chain (sc) Fv antibody fragment from a synthetic phage antibody display library was biosynthetically lipid-tagged by using Escherichia coli lipoprotein sequences [3].

High impact information on traH

• Escherichia coli Braun lipoprotein induces a lipopolysaccharide-like endotoxic response from primary human endothelial cells [4].
• It has been postulated that the N-acyl fatty acid attached to the amino terminus of the major Escherichia coli lipoprotein is derived from the fatty acid at the 1-position of phosphatidylethanolamine (PtdEtn) (Jackowski, S., and Rock, C.O. (1986) J. Biol. Chem. 261, 11328-11333) [5].
• A synthetic analogue of Escherichia coli lipoprotein, tripalmitoyl pentapeptide, constitutes a potent immune adjuvant [6].
• A protein analogous to Escherichia coli Braun lipoprotein was not detected with gonococcal cell wall preparations [7].
• Employing pssN-phoA and pssN-lacZ gene fusions and in vivo acylation with [(3)H]palmitate, we demonstrated that PssN is a 43-kDa lipoprotein directed to the periplasm by an N-terminal signal sequence [1].

Chemical compound and disease context of traH

• The mitogenic principle of Escherichia coli lipoprotein: B-lymphocyte mitogenicity of N-palmitoyl-cysteine and N-palmitoyl-glutamic acid alpha-methyl ester [8].
• The mitogenic principle of Escherichia coli lipoprotein: B-lymphocyte mitogenicity of the synthetic analogue palmitoyl-tetrapeptide (Pam-Ser-Ser-Asn-Ala) [9].

Biological context of traH

• Thus, the tra genes traH, G, T, and D were localized on the plasmid R100 [10].
• A site-specific mutation was made by the polymerase chain reaction-based unique-site mutagenesis procedure to alter the start site of traH [11].
• Induction kinetics and cell surface distribution of Escherichia coli lipoprotein under lac promoter control [12].
• It is concluded that the mechanism of acylation is different from that in Escherichia coli lipoprotein and Bacillus penicillinase [13].

Other interactions of traH

• Analysis of plasmid deletion derivatives that we constructed in vitro shows that these genes map in the order traF trbA traQ trbB traH [14].

Analytical, diagnostic and therapeutic context of traH

• The deletion of several codons within the signal sequence coding region of the Escherichia coli lipoprotein gene has been accomplished by oligonucleotide-directed site-specific mutagenesis [15].

References