Table of Contents Author Guidelines Submit a Manuscript
International Journal of Microbiology
Volume 2010 (2010), Article ID 187373, 21 pages
Research Article

Functional Promiscuity of Homologues of the Bacterial ArsA ATPases

Division of Biological Sciences, University of California at San Diego, La Jolla, CA 92093-0116, USA

Received 3 July 2010; Accepted 7 September 2010

Academic Editor: Ingolf Figved Nes

Copyright © 2010 Rostislav Castillo and Milton H. Saier. 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.


The ArsA ATPase of E. coli plays an essential role in arsenic detoxification. Published evidence implicates ArsA in the energization of As(III) efflux via the formation of an oxyanion-translocating complex with ArsB. In addition, eukaryotic ArsA homologues have several recognized functions unrelated to arsenic resistance. By aligning ArsA homologues, constructing phylogenetic trees, examining ArsA encoding operons, and estimating the probable coevolution of these homologues with putative transporters and auxiliary proteins unrelated to ArsB, we provide evidence for new functions for ArsA homologues. They may play roles in carbon starvation, gas vesicle biogenesis, and arsenic resistance. The results lead to the proposal that ArsA homologues energize four distinct and nonhomologous transporters, ArsB, ArsP, CstA, and Acr3.