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Membrane Porters of ATP-Binding Cassette Transport Systems Are Polyphyletic
The ATP-binding cassette (ABC) superfamily consists of both importers and exporters. These transporters have, by tradition, been classified according to the ATP hydrolyzing constituents, which are monophyletic. The evolutionary origins of the transmembrane porter proteins/domains are not known. Usin...
Autores principales: | , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
Springer-Verlag
2009
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2760711/ https://www.ncbi.nlm.nih.gov/pubmed/19418088 http://dx.doi.org/10.1007/s00232-009-9200-6 |
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author | Wang, Bin Dukarevich, Maxim Sun, Eric I. Yen, Ming Ren Saier, Milton H. |
author_facet | Wang, Bin Dukarevich, Maxim Sun, Eric I. Yen, Ming Ren Saier, Milton H. |
author_sort | Wang, Bin |
collection | PubMed |
description | The ATP-binding cassette (ABC) superfamily consists of both importers and exporters. These transporters have, by tradition, been classified according to the ATP hydrolyzing constituents, which are monophyletic. The evolutionary origins of the transmembrane porter proteins/domains are not known. Using five distinct computer programs, we here provide convincing statistical data suggesting that the transmembrane domains of ABC exporters are polyphyletic, having arisen at least three times independently. ABC1 porters arose by intragenic triplication of a primordial two-transmembrane segment (TMS)-encoding genetic element, yielding six TMS proteins. ABC2 porters arose by intragenic duplication of a dissimilar primordial three-TMS-encoding genetic element, yielding a distinctive protein family, nonhomologous to the ABC1 proteins. ABC3 porters arose by duplication of a primordial four-TMS-encoding genetic element, yielding either eight- or 10-TMS proteins. We assign each of 48 of the 50 currently recognized families of ABC exporters to one of the three evolutionarily distinct ABC types. Currently available high-resolution structural data for ABC porters are fully consistent with our findings. These results provide guides for future structural and mechanistic studies of these important transport systems. |
format | Text |
id | pubmed-2760711 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | Springer-Verlag |
record_format | MEDLINE/PubMed |
spelling | pubmed-27607112009-10-16 Membrane Porters of ATP-Binding Cassette Transport Systems Are Polyphyletic Wang, Bin Dukarevich, Maxim Sun, Eric I. Yen, Ming Ren Saier, Milton H. J Membr Biol Topical Review The ATP-binding cassette (ABC) superfamily consists of both importers and exporters. These transporters have, by tradition, been classified according to the ATP hydrolyzing constituents, which are monophyletic. The evolutionary origins of the transmembrane porter proteins/domains are not known. Using five distinct computer programs, we here provide convincing statistical data suggesting that the transmembrane domains of ABC exporters are polyphyletic, having arisen at least three times independently. ABC1 porters arose by intragenic triplication of a primordial two-transmembrane segment (TMS)-encoding genetic element, yielding six TMS proteins. ABC2 porters arose by intragenic duplication of a dissimilar primordial three-TMS-encoding genetic element, yielding a distinctive protein family, nonhomologous to the ABC1 proteins. ABC3 porters arose by duplication of a primordial four-TMS-encoding genetic element, yielding either eight- or 10-TMS proteins. We assign each of 48 of the 50 currently recognized families of ABC exporters to one of the three evolutionarily distinct ABC types. Currently available high-resolution structural data for ABC porters are fully consistent with our findings. These results provide guides for future structural and mechanistic studies of these important transport systems. Springer-Verlag 2009-10-06 2009-09 /pmc/articles/PMC2760711/ /pubmed/19418088 http://dx.doi.org/10.1007/s00232-009-9200-6 Text en © The Author(s) 2009 |
spellingShingle | Topical Review Wang, Bin Dukarevich, Maxim Sun, Eric I. Yen, Ming Ren Saier, Milton H. Membrane Porters of ATP-Binding Cassette Transport Systems Are Polyphyletic |
title | Membrane Porters of ATP-Binding Cassette Transport Systems Are Polyphyletic |
title_full | Membrane Porters of ATP-Binding Cassette Transport Systems Are Polyphyletic |
title_fullStr | Membrane Porters of ATP-Binding Cassette Transport Systems Are Polyphyletic |
title_full_unstemmed | Membrane Porters of ATP-Binding Cassette Transport Systems Are Polyphyletic |
title_short | Membrane Porters of ATP-Binding Cassette Transport Systems Are Polyphyletic |
title_sort | membrane porters of atp-binding cassette transport systems are polyphyletic |
topic | Topical Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2760711/ https://www.ncbi.nlm.nih.gov/pubmed/19418088 http://dx.doi.org/10.1007/s00232-009-9200-6 |
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