Structural and Functional Diversity of Two ATP-Driven Plant Proton Pumps
Two ATP-dependent proton pumps function in plant cells. Plasma membrane H<sup>+</sup>-ATPase (PM H<sup>+</sup>-ATPase) transfers protons from the cytoplasm to the apoplast, while vacuolar H<sup>+</sup>-ATPase (V-ATPase), located in tonoplasts and other endomembran...
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| Format: | Article |
| Language: | English |
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MDPI AG
2023-02-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/24/5/4512 |
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| author | Katarzyna Kabała Małgorzata Janicka |
| author_facet | Katarzyna Kabała Małgorzata Janicka |
| author_sort | Katarzyna Kabała |
| collection | DOAJ |
| description | Two ATP-dependent proton pumps function in plant cells. Plasma membrane H<sup>+</sup>-ATPase (PM H<sup>+</sup>-ATPase) transfers protons from the cytoplasm to the apoplast, while vacuolar H<sup>+</sup>-ATPase (V-ATPase), located in tonoplasts and other endomembranes, is responsible for proton pumping into the organelle lumen. Both enzymes belong to two different families of proteins and, therefore, differ significantly in their structure and mechanism of action. The plasma membrane H<sup>+</sup>-ATPase is a member of the P-ATPases that undergo conformational changes, associated with two distinct E1 and E2 states, and autophosphorylation during the catalytic cycle. The vacuolar H<sup>+</sup>-ATPase represents rotary enzymes functioning as a molecular motor. The plant V-ATPase consists of thirteen different subunits organized into two subcomplexes, the peripheral V<sub>1</sub> and the membrane-embedded V<sub>0</sub>, in which the stator and rotor parts have been distinguished. In contrast, the plant plasma membrane proton pump is a functional single polypeptide chain. However, when the enzyme is active, it transforms into a large twelve-protein complex of six H<sup>+</sup>-ATPase molecules and six 14-3-3 proteins. Despite these differences, both proton pumps can be regulated by the same mechanisms (such as reversible phosphorylation) and, in some processes, such as cytosolic pH regulation, may act in a coordinated way. |
| first_indexed | 2024-03-11T07:22:40Z |
| format | Article |
| id | doaj.art-7afaea090ac5405799d171b145188f9e |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-11T07:22:40Z |
| publishDate | 2023-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-7afaea090ac5405799d171b145188f9e2023-11-17T07:49:31ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672023-02-01245451210.3390/ijms24054512Structural and Functional Diversity of Two ATP-Driven Plant Proton PumpsKatarzyna Kabała0Małgorzata Janicka1Department of Plant Molecular Physiology, Faculty of Biological Sciences, University of Wrocław, Kanonia 6/8, 50-328 Wrocław, PolandDepartment of Plant Molecular Physiology, Faculty of Biological Sciences, University of Wrocław, Kanonia 6/8, 50-328 Wrocław, PolandTwo ATP-dependent proton pumps function in plant cells. Plasma membrane H<sup>+</sup>-ATPase (PM H<sup>+</sup>-ATPase) transfers protons from the cytoplasm to the apoplast, while vacuolar H<sup>+</sup>-ATPase (V-ATPase), located in tonoplasts and other endomembranes, is responsible for proton pumping into the organelle lumen. Both enzymes belong to two different families of proteins and, therefore, differ significantly in their structure and mechanism of action. The plasma membrane H<sup>+</sup>-ATPase is a member of the P-ATPases that undergo conformational changes, associated with two distinct E1 and E2 states, and autophosphorylation during the catalytic cycle. The vacuolar H<sup>+</sup>-ATPase represents rotary enzymes functioning as a molecular motor. The plant V-ATPase consists of thirteen different subunits organized into two subcomplexes, the peripheral V<sub>1</sub> and the membrane-embedded V<sub>0</sub>, in which the stator and rotor parts have been distinguished. In contrast, the plant plasma membrane proton pump is a functional single polypeptide chain. However, when the enzyme is active, it transforms into a large twelve-protein complex of six H<sup>+</sup>-ATPase molecules and six 14-3-3 proteins. Despite these differences, both proton pumps can be regulated by the same mechanisms (such as reversible phosphorylation) and, in some processes, such as cytosolic pH regulation, may act in a coordinated way.https://www.mdpi.com/1422-0067/24/5/4512plant proton pumpplasma membrane H<sup>+</sup>-ATPaseproton gradientvacuolar H<sup>+</sup>-ATPase |
| spellingShingle | Katarzyna Kabała Małgorzata Janicka Structural and Functional Diversity of Two ATP-Driven Plant Proton Pumps International Journal of Molecular Sciences plant proton pump plasma membrane H<sup>+</sup>-ATPase proton gradient vacuolar H<sup>+</sup>-ATPase |
| title | Structural and Functional Diversity of Two ATP-Driven Plant Proton Pumps |
| title_full | Structural and Functional Diversity of Two ATP-Driven Plant Proton Pumps |
| title_fullStr | Structural and Functional Diversity of Two ATP-Driven Plant Proton Pumps |
| title_full_unstemmed | Structural and Functional Diversity of Two ATP-Driven Plant Proton Pumps |
| title_short | Structural and Functional Diversity of Two ATP-Driven Plant Proton Pumps |
| title_sort | structural and functional diversity of two atp driven plant proton pumps |
| topic | plant proton pump plasma membrane H<sup>+</sup>-ATPase proton gradient vacuolar H<sup>+</sup>-ATPase |
| url | https://www.mdpi.com/1422-0067/24/5/4512 |
| work_keys_str_mv | AT katarzynakabała structuralandfunctionaldiversityoftwoatpdrivenplantprotonpumps AT małgorzatajanicka structuralandfunctionaldiversityoftwoatpdrivenplantprotonpumps |