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The plasma membrane H(+)‐ATPase, a simple polypeptide with a long history
The plasma membrane H(+)‐ATPase of fungi and plants is a single polypeptide of fewer than 1,000 residues that extrudes protons from the cell against a large electric and concentration gradient. The minimalist structure of this nanomachine is in stark contrast to that of the large multi‐subunit F(O)F...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2018
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6590192/ https://www.ncbi.nlm.nih.gov/pubmed/30447028 http://dx.doi.org/10.1002/yea.3365 |
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author | Palmgren, Michael Morsomme, Pierre |
author_facet | Palmgren, Michael Morsomme, Pierre |
author_sort | Palmgren, Michael |
collection | PubMed |
description | The plasma membrane H(+)‐ATPase of fungi and plants is a single polypeptide of fewer than 1,000 residues that extrudes protons from the cell against a large electric and concentration gradient. The minimalist structure of this nanomachine is in stark contrast to that of the large multi‐subunit F(O)F(1) ATPase of mitochondria, which is also a proton pump, but under physiological conditions runs in the reverse direction to act as an ATP synthase. The plasma membrane H(+)‐ATPase is a P‐type ATPase, defined by having an obligatory phosphorylated reaction cycle intermediate, like cation pumps of animal membranes, and thus, this pump has a completely different mechanism to that of F(O)F(1) ATPases, which operates by rotary catalysis. The work that led to these insights in plasma membrane H(+)‐ATPases of fungi and plants has a long history, which is briefly summarized in this review. |
format | Online Article Text |
id | pubmed-6590192 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-65901922019-07-08 The plasma membrane H(+)‐ATPase, a simple polypeptide with a long history Palmgren, Michael Morsomme, Pierre Yeast Special Issue Articles The plasma membrane H(+)‐ATPase of fungi and plants is a single polypeptide of fewer than 1,000 residues that extrudes protons from the cell against a large electric and concentration gradient. The minimalist structure of this nanomachine is in stark contrast to that of the large multi‐subunit F(O)F(1) ATPase of mitochondria, which is also a proton pump, but under physiological conditions runs in the reverse direction to act as an ATP synthase. The plasma membrane H(+)‐ATPase is a P‐type ATPase, defined by having an obligatory phosphorylated reaction cycle intermediate, like cation pumps of animal membranes, and thus, this pump has a completely different mechanism to that of F(O)F(1) ATPases, which operates by rotary catalysis. The work that led to these insights in plasma membrane H(+)‐ATPases of fungi and plants has a long history, which is briefly summarized in this review. John Wiley and Sons Inc. 2018-12-10 2019-04 /pmc/articles/PMC6590192/ /pubmed/30447028 http://dx.doi.org/10.1002/yea.3365 Text en © 2018 The Authors. Yeast published by John Wiley & Sons, Ltd. This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Special Issue Articles Palmgren, Michael Morsomme, Pierre The plasma membrane H(+)‐ATPase, a simple polypeptide with a long history |
title | The plasma membrane H(+)‐ATPase, a simple polypeptide with a long history |
title_full | The plasma membrane H(+)‐ATPase, a simple polypeptide with a long history |
title_fullStr | The plasma membrane H(+)‐ATPase, a simple polypeptide with a long history |
title_full_unstemmed | The plasma membrane H(+)‐ATPase, a simple polypeptide with a long history |
title_short | The plasma membrane H(+)‐ATPase, a simple polypeptide with a long history |
title_sort | plasma membrane h(+)‐atpase, a simple polypeptide with a long history |
topic | Special Issue Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6590192/ https://www.ncbi.nlm.nih.gov/pubmed/30447028 http://dx.doi.org/10.1002/yea.3365 |
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