bacterial adaptor membrane fusion proteins and the structurally dissimilar outer membrane auxiliary proteins have exchanged central domains in -proteobacteria细菌适配器膜融合蛋白和蛋白质结构不同的外膜辅助交换中心域变形菌门.pdfVIP

Hindawi Publishing Corporation International Journal of Microbiology Volume 2010, Article ID 589391, 5 pages doi:10.1155/2010/589391 Research Article Bacterial Adaptor Membrane Fusion Proteins and the Structurally Dissimilar Outer Membrane Auxiliary Proteins Have Exchanged Central Domains in α-Proteobacteria Anthony Y. Xiao, Jing Wang, and Milton H. Saier Jr. Division of Biological Sciences, University of California at San Diego, La Jolla, CA 92093-0116, USA Correspondence should be addressed to Milton H. Saier Jr., msaier@ Received 10 December 2009; Accepted 31 January 2010 ´ Academic Editor: Isabel Sa-Correia Copyright © 2010 Anthony Y. Xiao et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Transport systems frequently include auxiliary proteins that perform subfunctions within the transporter protein complex. Two such proteins found in Gram-negative bacteria are the Membrane Fusion Proteins (MFPs) and the Outer Membrane Auxiliary (OMA) proteins. We here demonstrate that OMAs present in α-proteobacteria (but not in other bacterial types) contain a long α-helical region that is homologous to corresponding regions in the MFPs. The results suggest that during their evolution, OMAs, specifically from α-proteobacteria, exchanged their own α-helical domain for one derived from an MFP. The structural and functional implications of these findings are discussed. 1. Introduction milieu without equilibration of solutes in the periplasm, all