Open AccessProtein secretion and outer membrane assembly in Alphaproteobacteria
Author(s) -
Gatsos Xenia,
Perry Andrew J.,
Anwari Khatira,
Dolezal Pavel,
Wolynec P. Peter,
Likić Vladimir A.,
Purcell Anthony W.,
Buchanan Susan K.,
Lithgow Trevor
Publication year - 2008
Publication title -
fems microbiology reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.91
H-Index - 212
eISSN - 1574-6976
pISSN - 0168-6445
DOI - 10.1111/j.1574-6976.2008.00130.x
Subject(s) - bacterial outer membrane , alphaproteobacteria , biology , tetratricopeptide , translocase of the outer membrane , periplasmic space , biogenesis , cardiolipin , bacteria , cell envelope , escherichia coli , biochemistry , microbiology and biotechnology , genetics , gene , membrane , 16s ribosomal rna , phospholipid
The assembly of β‐barrel proteins into membranes is a fundamental process that is essential in Gram‐negative bacteria, mitochondria and plastids. Our understanding of the mechanism of β‐barrel assembly is progressing from studies carried out in Escherichia coli and Neisseria meningitidis . Comparative sequence analysis suggests that while many components mediating β‐barrel protein assembly are conserved in all groups of bacteria with outer membranes, some components are notably absent. The Alphaproteobacteria in particular seem prone to gene loss and show the presence or absence of specific components mediating the assembly of β‐barrels: some components of the pathway appear to be missing from whole groups of bacteria (e.g. Skp, YfgL and NlpB), other proteins are conserved but are missing characteristic domains (e.g. SurA). This comparative analysis is also revealing important structural signatures that are vague unless multiple members from a protein family are considered as a group (e.g. tetratricopeptide repeat (TPR) motifs in YfiO, β‐propeller signatures in YfgL). Given that the process of the β‐barrel assembly is conserved, analysis of outer membrane biogenesis in Alphaproteobacteria , the bacterial group that gave rise to mitochondria, also promises insight into the assembly of β‐barrel proteins in eukaryotes.