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Related Concept Videos

ATP Driven Pumps III: V-type Pumps01:30

ATP Driven Pumps III: V-type Pumps

3.9K
V-type pumps are ATP-driven pumps found in the vacuolar membranes of plants, yeast, endosomal and lysosomal membranes of animal cells, plasma membranes of a few specialized eukaryotic cells, and some prokaryotes. They are also known as the V1Vo-ATPase, that couple ATP hydrolysis to transport protons against a concentration gradient.
The peripheral or cytosolic V1 domain with eight subunits is involved in ATP hydrolysis. The integral or transmembrane V0 domain containing at least five subunits...
3.9K
ATP Driven Pumps I: An Overview01:27

ATP Driven Pumps I: An Overview

8.5K
ATP-driven pumps, also known as transport ATPases, are integral membrane proteins. They have binding sites for ATP located on the membrane's cytosolic side and the ion-conducting domain in the transmembrane region. These pumps use the free energy released from ATP hydrolysis to move the solutes across cell membranes against an electrochemical gradient.
There are four main types of ATP-driven pumps - P-type, V-type, F-type, and ABC transporter. All these pumps are of varying complexities and...
8.5K
ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

15.1K
In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...
15.1K
ATP Driven Pumps II: P-type Pumps01:34

ATP Driven Pumps II: P-type Pumps

5.1K
The P-type pumps are a large family of integral membrane transporter ATPases. They are divided into five major types based on substrate specificity, from I to V.
A typical P-type pump has three cytosolic domains: nucleotide-binding (N), phosphorylation (P), and activator (A) domains. These domains are connected to the membrane-spanning helices by short amino acid segments. ATP hydrolysis and covalent phosphoenzyme intermediate formation are crucial parts of the catalytic cycle. At the highly...
5.1K
Hydrolysis of ATP01:08

Hydrolysis of ATP

76.7K
The bonds of adenosine triphosphate (ATP) can be broken through the addition of water, releasing one or two phosphate groups in an exergonic process called hydrolysis. This reaction liberates the energy in the bonds for use in the cell—for instance, to synthesize proteins from amino acids.
If one phosphate group is removed, a molecule of ADP—adenosine diphosphate—remains, along with inorganic phosphate. ADP can be further hydrolyzed to AMP—adenosine...
76.7K
ATP Yield01:31

ATP Yield

71.3K
Cellular respiration produces 30 - 32 ATP per glucose molecule. Although most of the ATP results from oxidative phosphorylation and the electron transport chain (ETC), 4 ATP are gained beforehand (2 from glycolysis and 2 from the citric acid cycle).
The ETC is embedded in the inner mitochondrial membrane and is comprised of four main protein complexes and an ATP synthase. NADH and FADH2 pass electrons to these complexes, which pump protons into the intermembrane space. This distribution of...
71.3K

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Measuring In Vitro ATPase Activity for Enzymatic Characterization
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Measuring In Vitro ATPase Activity for Enzymatic Characterization

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The Plant V-ATPase.

Thorsten Seidel1

  • 1Dynamic Cell Imaging, Faculty of Biology, Bielefeld University, Bielefeld, Germany.

Frontiers in Plant Science
|July 18, 2022
PubMed
Summary
This summary is machine-generated.

Plant vacuolar ATPase (V-ATPase) is vital for cell pH and stress response. Understanding its complex regulation offers potential for improving crop yield and stress resistance.

Keywords:
ArabidopsisV-ATPaseglucosepH-homeostasisproton pump

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Area of Science:

  • Plant cell biology
  • Molecular plant science

Background:

  • Vacuolar H+-translocating ATPase (V-ATPase) is a key proton pump in plant cells, essential for maintaining cytosolic pH homeostasis.
  • It energizes transport across endomembranes, crucial for the secretory pathway, including cell wall component delivery and stress responses.
  • The V-ATPase's complex structure and isoform diversity allow adaptability but necessitate sophisticated assembly and transport mechanisms, which remain incompletely understood.

Purpose of the Study:

  • To review the current understanding of V-ATPase structure, function, and regulation in plants.
  • To highlight the importance of V-ATPase localization and activity in plant physiology and stress adaptation.
  • To identify V-ATPase regulation as a potential target for enhancing crop traits.

Main Methods:

  • Literature review and synthesis of existing research on plant V-ATPase.
  • Analysis of V-ATPase's role in cellular processes like pH homeostasis and vesicle transport.
  • Examination of known regulatory mechanisms including post-translational modifications and protein interactions.

Main Results:

  • V-ATPase localization in the trans-Golgi network/early endosomes is critical for vesicle transport and cell wall formation.
  • The enzyme plays a significant role in plant responses to both abiotic and biotic stresses.
  • Regulation involves phosphorylation, redox modifications, protein interactions (e.g., 14-3-3 proteins), and lipid environment, but reversible assembly, unlike in yeast/mammals, appears absent in autotrophic plant cells.

Conclusions:

  • Understanding V-ATPase regulation is crucial for harnessing its potential in plant science.
  • Targeting V-ATPase activity offers a promising strategy for improving plant stress resistance and crop yield.
  • Further research into the assembly and regulatory machinery of plant V-ATPases is warranted.