Functional Promiscuity of Homologues of the Bacterial ArsA ATPases
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...
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| Format: | Article |
| Language: | English |
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Wiley
2010-01-01
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| Series: | International Journal of Microbiology |
| Online Access: | http://dx.doi.org/10.1155/2010/187373 |
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| _version_ | 1849306681594347520 |
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| author | Rostislav Castillo Milton H. Saier |
| author_facet | Rostislav Castillo Milton H. Saier |
| author_sort | Rostislav Castillo |
| collection | DOAJ |
| description | 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. |
| format | Article |
| id | doaj-art-25fd9d8dedaf498f86ce71ab5b6025a4 |
| institution | Kabale University |
| issn | 1687-918X 1687-9198 |
| language | English |
| publishDate | 2010-01-01 |
| publisher | Wiley |
| record_format | Article |
| series | International Journal of Microbiology |
| spelling | doaj-art-25fd9d8dedaf498f86ce71ab5b6025a42025-08-20T03:55:00ZengWileyInternational Journal of Microbiology1687-918X1687-91982010-01-01201010.1155/2010/187373187373Functional Promiscuity of Homologues of the Bacterial ArsA ATPasesRostislav Castillo0Milton H. Saier1Division of Biological Sciences, University of California at San Diego, La Jolla, CA 92093-0116, USADivision of Biological Sciences, University of California at San Diego, La Jolla, CA 92093-0116, USAThe 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.http://dx.doi.org/10.1155/2010/187373 |
| spellingShingle | Rostislav Castillo Milton H. Saier Functional Promiscuity of Homologues of the Bacterial ArsA ATPases International Journal of Microbiology |
| title | Functional Promiscuity of Homologues of the Bacterial ArsA ATPases |
| title_full | Functional Promiscuity of Homologues of the Bacterial ArsA ATPases |
| title_fullStr | Functional Promiscuity of Homologues of the Bacterial ArsA ATPases |
| title_full_unstemmed | Functional Promiscuity of Homologues of the Bacterial ArsA ATPases |
| title_short | Functional Promiscuity of Homologues of the Bacterial ArsA ATPases |
| title_sort | functional promiscuity of homologues of the bacterial arsa atpases |
| url | http://dx.doi.org/10.1155/2010/187373 |
| work_keys_str_mv | AT rostislavcastillo functionalpromiscuityofhomologuesofthebacterialarsaatpases AT miltonhsaier functionalpromiscuityofhomologuesofthebacterialarsaatpases |