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. / Palmgren, Michael; Morsomme, Pierre.

In: Yeast, Vol. 36, No. 4, 04.2019, p. 201-210.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Palmgren, M & Morsomme, P 2019, 'The plasma membrane H+-ATPase, a simple polypeptide with a long history', Yeast, vol. 36, no. 4, pp. 201-210. https://doi.org/10.1002/yea.3365

APA

Palmgren, M., & Morsomme, P. (2019). The plasma membrane H+-ATPase, a simple polypeptide with a long history. Yeast, 36(4), 201-210. https://doi.org/10.1002/yea.3365

Vancouver

Palmgren M, Morsomme P. The plasma membrane H+-ATPase, a simple polypeptide with a long history. Yeast. 2019 Apr;36(4):201-210. https://doi.org/10.1002/yea.3365

Author

Palmgren, Michael ; Morsomme, Pierre. / The plasma membrane H+-ATPase, a simple polypeptide with a long history. In: Yeast. 2019 ; Vol. 36, No. 4. pp. 201-210.

Bibtex

@article{f323284da33446fa86497c7a4e00bb1c,
title = "The plasma membrane H+-ATPase, a simple polypeptide with a long history",
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 FOF1 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 FOF1 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, proton pump, Saccharomyces cerevisiae, Schizosaccharomyces pombe",
author = "Michael Palmgren and Pierre Morsomme",
year = "2019",
month = apr,
doi = "10.1002/yea.3365",
language = "English",
volume = "36",
pages = "201--210",
journal = "Yeast",
issn = "0749-503X",
publisher = "JohnWiley & Sons Ltd",
number = "4",

}

RIS

TY - JOUR

T1 - The plasma membrane H+-ATPase, a simple polypeptide with a long history

AU - Palmgren, Michael

AU - Morsomme, Pierre

PY - 2019/4

Y1 - 2019/4

N2 - 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 FOF1 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 FOF1 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.

AB - 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 FOF1 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 FOF1 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.

KW - Arabidopsis thaliana

KW - F-type ATPase

KW - Neurospora crassa

KW - Nicotiana tabacum

KW - P-type ATPase

KW - proton pump

KW - Saccharomyces cerevisiae

KW - Schizosaccharomyces pombe

U2 - 10.1002/yea.3365

DO - 10.1002/yea.3365

M3 - Journal article

C2 - 30447028

AN - SCOPUS:85058038743

VL - 36

SP - 201

EP - 210

JO - Yeast

JF - Yeast

SN - 0749-503X

IS - 4

ER -

ID: 213856468