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dc.contributor.authorSutcliffe, I.C.*
dc.contributor.authorHarrington, Dean J.*
dc.contributor.authorHutchings, M.I.*
dc.date.accessioned2017-03-08T12:11:07Z
dc.date.available2017-03-08T12:11:07Z
dc.date.issued2012-03
dc.identifier.citationSutcliffe IC, Harrington DJ and Hutchings MI (2012) A phylum level analysis reveals lipoprotein biosynthesis to be a fundamental property of bacteria. Protein and Cell. 3(3): 163-170.en_US
dc.identifier.urihttp://hdl.handle.net/10454/11567
dc.descriptionNoen_US
dc.description.abstractBacterial lipoproteins are proteins that are post-translationally modified with a diacylglyceride at an N-terminal cysteine, which serves to tether these proteins to the outer face of the plasma membrane or to the outer membrane. This paper reviews recent insights into the enzymology of bacterial lipoprotein biosynthesis and localization. Moreover, we use bioinformatic analyses of bacterial lipoprotein signal peptide features and of the key biosynthetic enzymes to consider the distribution of lipoprotein biosynthesis at the phylum level. These analyses support the important conclusion that lipoprotein biosynthesis is a fundamental pathway utilized across the domain bacteria. Moreover, with the exception of a small number of sequences likely to derive from endosymbiont genomes, the enzymes of bacterial lipoprotein biosynthesis appear unique to bacteria, making this pathway an attractive target for the development of novel antimicrobials. Whilst lipoproteins with comparable signal peptide features are encoded in the genomes of Archaea, it is clear that these lipoproteins have a distinctive biosynthetic pathway that has yet to be characterized.en_US
dc.language.isoenen_US
dc.subjectLipoprotein biosynthesis; Bacteria; Antimicrobialsen_US
dc.titleA phylum level analysis reveals lipoprotein biosynthesis to be a fundamental property of bacteriaen_US
dc.status.refereedYesen_US
dc.date.application2012-03-10
dc.typeArticleen_US
dc.type.versionNo full-text in the repositoryen_US
dc.identifier.doihttps://doi.org/10.1007/s13238-012-2023-8


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