Protein secretion and outer membrane assembly in Alphaproteobacteria Export

@article{citeulike:3196685, abstract = {The assembly of 03B2-barrel proteins into membranes is a fundamental process that is essential in Gram-negative bacteria, mitochondria and plastids. Our understanding of the mechanism of 03B2-barrel assembly is progressing from studies carried out in Escherichia coli and Neisseria meningitidis. Comparative sequence analysis suggests that while many components mediating 03B2-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 03B2-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, 03B2-propeller signatures in YfgL). Given that the process of the 03B2-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 03B2-barrel proteins in eukaryotes.}, address = {Department of Biochemistry and Molecular Biology, University of Melbourne, Melbourne, Australia; Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Melbourne, Australia; Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, USA}, author = {Gatsos, Xenia and Perry, Andrew J. and Anwari, Khatira and Dolezal, Pavel and Wolynec, Peter P. and Liki0107, Vladimir A. and Purcell, Anthony W. and Buchanan, Susan K. and Lithgow, Trevor}, citeulike-article-id = {3196685}, citeulike-linkout-0 = {http://dx.doi.org/10.1111/j.1574-6976.2008.00130.x}, citeulike-linkout-1 = {http://www3.interscience.wiley.com/cgi-bin/abstract/121390723/ABSTRACT}, doi = {10.1111/j.1574-6976.2008.00130.x}, journal = {FEMS Microbiology Reviews}, keywords = {alphaproteobacteria, bacteria, beta-barrel, membrane, secretion}, number = {9999}, posted-at = {2008-09-05 05:45:46}, priority = {2}, title = {Protein secretion and outer membrane assembly in Alphaproteobacteria}, url = {http://dx.doi.org/10.1111/j.1574-6976.2008.00130.x}, volume = {9999}, year = {2008} }

TY - JOUR ID - citeulike:3196685 L3 - citeulike-article-id:3196685 N2 - The assembly of 03B2-barrel proteins into membranes is a fundamental process that is essential in Gram-negative bacteria, mitochondria and plastids. Our understanding of the mechanism of 03B2-barrel assembly is progressing from studies carried out in Escherichia coli and Neisseria meningitidis. Comparative sequence analysis suggests that while many components mediating 03B2-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 03B2-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, 03B2-propeller signatures in YfgL). Given that the process of the 03B2-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 03B2-barrel proteins in eukaryotes. IS - 9999 JF - FEMS Microbiology Reviews AD - Department of Biochemistry and Molecular Biology, University of Melbourne, Melbourne, Australia; Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Melbourne, Australia; Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, USA TI - Protein secretion and outer membrane assembly in Alphaproteobacteria VL - 9999 KW - alphaproteobacteria KW - bacteria KW - beta-barrel KW - membrane KW - secretion AU - Gatsos, Xenia AU - Perry, Andrew AU - Anwari, Khatira AU - Dolezal, Pavel AU - Wolynec, Peter AU - Liki0107, Vladimir AU - Purcell, Anthony AU - Buchanan, Susan AU - Lithgow, Trevor PY - 2008/// UR - http://dx.doi.org/10.1111/j.1574-6976.2008.00130.x ER -