The plasma membrane H+ -ATPase, a simple polypeptide with a long history

doi:10.1002/yea.3365

Review

. 2019 Apr;36(4):201-210.

doi: 10.1002/yea.3365. Epub 2018 Dec 10.

The plasma membrane H⁺ -ATPase, a simple polypeptide with a long history

Michael Palmgren¹, Pierre Morsomme²

Affiliations

¹ Department of Plant and Environmental Sciences, University of Copenhagen, Frederiksberg C, Denmark.
² Louvain Institute of Biomolecular Science and Technology (LIBST), UCLouvain, Louvain-la-Neuve, Belgium.

PMID: 30447028
PMCID: PMC6590192
DOI: 10.1002/yea.3365

Free PMC article

Review

The plasma membrane H⁺ -ATPase, a simple polypeptide with a long history

Michael Palmgren et al. Yeast. 2019 Apr.

Free PMC article

. 2019 Apr;36(4):201-210.

doi: 10.1002/yea.3365. Epub 2018 Dec 10.

Authors

Michael Palmgren¹, Pierre Morsomme²

Affiliations

¹ Department of Plant and Environmental Sciences, University of Copenhagen, Frederiksberg C, Denmark.
² Louvain Institute of Biomolecular Science and Technology (LIBST), UCLouvain, Louvain-la-Neuve, Belgium.

PMID: 30447028
PMCID: PMC6590192
DOI: 10.1002/yea.3365

Abstract

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 F₁ 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 F₁ 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.

Keywords: Arabidopsis thaliana; F-type ATPase; Neurospora crassa; Nicotiana tabacum; P-type ATPase; Saccharomyces cerevisiae; Schizosaccharomyces pombe; proton pump.

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References

1. Addison, R. (1986). Primary structure of the Neurospora plasma membrane H+‐ATPase deduced from the gene sequence. Homology to Na+/K+‐, Ca2+‐, and K+‐ATPase. The Journal of Biological Chemistry, 261, 14896–14901. - PubMed
1. Amory, A. , Foury, F. , & Goffeau, A. (1980). The purified plasma membrane ATPase of the yeast Schizosaccharomyces pombe forms a phosphorylated intermediate. The Journal of Biological Chemistry, 255, 9353–9357. - PubMed
1. Arango, M. , Gévaudant, F. , Oufattole, M. , & Boutry, M. (2003). The plasma membrane proton pump ATPase: The significance of gene subfamilies. Planta, 216, 355–365. - PubMed
1. Axelsen, K. B. , Venema, K. , Jahn, T. , Baunsgaard, L. , & Palmgren, M. G. (1999). Molecular dissection of the C‐terminal regulatory domain of the plant plasma membrane H+‐ATPase AHA2: Mapping of residues that when altered give rise to an activated enzyme. Biochemistry, 38, 7227–7234. 10.1021/bi982482l - DOI - PubMed
1. Azzi, A. , Fabbro, A. , Santato, M. , & Gherardini, P. L. (1971). Energy transduction in mitochondrial fragments. Interaction of the membrane with acridine dyes. European Journal of Biochemistry, 21, 404–410. 10.1111/j.1432-1033.1971.tb01484.x - DOI - PubMed

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[1] Addison, R. (1986). Primary structure of the Neurospora plasma membrane H+‐ATPase deduced from the gene sequence. Homology to Na+/K+‐, Ca2+‐, and K+‐ATPase. The Journal of Biological Chemistry, 261, 14896–14901. - PubMed

[2] Addison, R. (1986). Primary structure of the Neurospora plasma membrane H+‐ATPase deduced from the gene sequence. Homology to Na+/K+‐, Ca2+‐, and K+‐ATPase. The Journal of Biological Chemistry, 261, 14896–14901. - PubMed

[3] Amory, A. , Foury, F. , & Goffeau, A. (1980). The purified plasma membrane ATPase of the yeast Schizosaccharomyces pombe forms a phosphorylated intermediate. The Journal of Biological Chemistry, 255, 9353–9357. - PubMed

[4] Amory, A. , Foury, F. , & Goffeau, A. (1980). The purified plasma membrane ATPase of the yeast Schizosaccharomyces pombe forms a phosphorylated intermediate. The Journal of Biological Chemistry, 255, 9353–9357. - PubMed

[5] Arango, M. , Gévaudant, F. , Oufattole, M. , & Boutry, M. (2003). The plasma membrane proton pump ATPase: The significance of gene subfamilies. Planta, 216, 355–365. - PubMed

[6] Arango, M. , Gévaudant, F. , Oufattole, M. , & Boutry, M. (2003). The plasma membrane proton pump ATPase: The significance of gene subfamilies. Planta, 216, 355–365. - PubMed

[7] Axelsen, K. B. , Venema, K. , Jahn, T. , Baunsgaard, L. , & Palmgren, M. G. (1999). Molecular dissection of the C‐terminal regulatory domain of the plant plasma membrane H+‐ATPase AHA2: Mapping of residues that when altered give rise to an activated enzyme. Biochemistry, 38, 7227–7234. 10.1021/bi982482l - DOI - PubMed

[8] Axelsen, K. B. , Venema, K. , Jahn, T. , Baunsgaard, L. , & Palmgren, M. G. (1999). Molecular dissection of the C‐terminal regulatory domain of the plant plasma membrane H+‐ATPase AHA2: Mapping of residues that when altered give rise to an activated enzyme. Biochemistry, 38, 7227–7234. 10.1021/bi982482l - DOI - PubMed

[9] Azzi, A. , Fabbro, A. , Santato, M. , & Gherardini, P. L. (1971). Energy transduction in mitochondrial fragments. Interaction of the membrane with acridine dyes. European Journal of Biochemistry, 21, 404–410. 10.1111/j.1432-1033.1971.tb01484.x - DOI - PubMed

[10] Azzi, A. , Fabbro, A. , Santato, M. , & Gherardini, P. L. (1971). Energy transduction in mitochondrial fragments. Interaction of the membrane with acridine dyes. European Journal of Biochemistry, 21, 404–410. 10.1111/j.1432-1033.1971.tb01484.x - DOI - PubMed

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The plasma membrane H⁺ -ATPase, a simple polypeptide with a long history

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The plasma membrane H⁺ -ATPase, a simple polypeptide with a long history

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