A phylum level analysis reveals lipoprotein biosynthesis to be a fundamental property of bacteria

Iain Sutcliffe, Dean Harrington, Matthew Hutchings

Research output: Contribution to journalArticlepeer-review

28 Citations (Scopus)

Abstract

Bacterial 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.
Original languageEnglish
Pages (from-to)163-170
JournalProtein & Cell
Volume3
Issue number3
DOIs
Publication statusPublished - Mar 2012

Fingerprint Dive into the research topics of 'A phylum level analysis reveals lipoprotein biosynthesis to be a fundamental property of bacteria'. Together they form a unique fingerprint.

Cite this