Linked Life Data

15611102

Source:http://linkedlifedata.com/resource/pubmed/id/15611102

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pubmed-article:15611102pubmed:abstractTextLipopolysaccharide (LPS) is one of the main constituents of the Gram-negative bacterial outer membrane. It usually consists of a highly variable O-antigen, a less variable core oligosaccharide, and a highly conserved lipid moiety, designated lipid A. Several bacteria are capable of modifying their lipid A architecture in response to external stimuli. The outer membrane-localized lipid A 3-O-deacylase, encoded by the pagL gene of Salmonella enterica serovar Typhimurium, removes the fatty acyl chain from the 3 position of lipid A. Although a similar activity was reported in some other Gram-negative bacteria, the corresponding genes could not be identified. Here, we describe the presence of pagL homologs in a variety of Gram-negative bacteria. Although the overall sequence similarity is rather low, a conserved domain could be distinguished in the C-terminal region. The activity of the Pseudomonas aeruginosa and Bordetella bronchiseptica pagL homologs was confirmed upon expression in Escherichia coli, which resulted in the removal of an R-3-hydroxymyristoyl group from lipid A. Upon deacylation by PagL, E. coli lipid A underwent another modification, which was the result of the activity of the endogenous palmitoyl transferase PagP. Furthermore, we identified a conserved histidine-serine couple as active site residues, suggesting a catalytic mechanism similar to serine hydrolases. The biological function of PagL remains unclear. However, because PagL homologs were found in both pathogenic and nonpathogenic species, PagL-mediated deacylation of lipid A probably does not have a dedicated role in pathogenicity.lld:pubmed
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pubmed-article:15611102pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:15611102pubmed:year2005lld:pubmed
pubmed-article:15611102pubmed:articleTitleDissemination of lipid A deacylases (pagL) among gram-negative bacteria: identification of active-site histidine and serine residues.lld:pubmed
pubmed-article:15611102pubmed:affiliationDepartment of Molecular Microbiology, Utrecht University, Padualaan 8, Utrecht 3584 CH, The Netherlands. j.j.g.geurtsen@bio.uu.nllld:pubmed
pubmed-article:15611102pubmed:publicationTypeJournal Articlelld:pubmed
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