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Related Concept Videos

ATP Synthase: Structure01:18

ATP Synthase: Structure

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ATP synthase or ATPase is among the most conserved proteins found in bacteria, mammals, and plants. This enzyme can catalyze a forward reaction in response to the electrochemical gradient, producing ATP from ADP and inorganic phosphate. ATP synthase can also work in a reverse direction by hydrolyzing ATP and generating an electrochemical gradient. Different forms of ATP synthases have evolved special features to meet the specific demands of the cell. Based on their specific feature, ATP...
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ATP Synthase: Mechanism01:48

ATP Synthase: Mechanism

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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...
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ATP Driven Pumps III: V-type Pumps01:30

ATP Driven Pumps III: V-type Pumps

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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...
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ATP Driven Pumps I: An Overview01:27

ATP Driven Pumps I: An Overview

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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...
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The ADP/ATP Carrier Protein01:42

The ADP/ATP Carrier Protein

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ADP/ATP carrier or AAC protein is the most abundant carrier protein in the inner mitochondrial membrane. It transports large quantities of ADP and ATP, equivalent to the average human body weight, every day. Among other transporters, ACC protein is one of the best-studied members of the mitochondrial carrier protein family. The ADP/ATP carrier protein comprises two transmembrane helices connected to a loop and a single alpha-helix on the matrix side. It switches between two conformational...
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Electron Transport Chain: Complex I and II01:46

Electron Transport Chain: Complex I and II

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The mitochondrial electron transport chain (ETC) is the main energy generation system in the eukaryotic cells. However, mitochondria also produce cytotoxic reactive oxygen species (ROS) due to the large electron flow during oxidative phosphorylation. While Complex I is one of the primary sources of superoxide radicals, ROS production by Complex II is uncommon and may only be observed in cancer cells with mutated complexes.
ROS generation is regulated and maintained at moderate levels necessary...
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Related Experiment Video

Updated: Sep 26, 2025

Visualization of ATP Synthase Dimers in Mitochondria by Electron Cryo-tomography
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Intersubunit and intrasubunit interactions driving the MukBEF ATPase.

Soon Bahng1, Rupesh Kumar1, Kenneth J Marians1

  • 1Molecular Biology Program, Memorial Sloan Kettering Cancer Center, New York, New York, USA.

The Journal of Biological Chemistry
|April 22, 2022
PubMed
Summary
This summary is machine-generated.

MukBEF, a bacterial condensin, compacts DNA using ATP hydrolysis. Key interactions within MukBEF and with topoisomerase IV regulate its ATPase activity, crucial for DNA condensation and cell viability.

Keywords:
ATPaseDNA structureDNA-binding proteingenome structurenucleic acid enzymology

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Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET
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Isolation of F1-ATPase from the Parasitic Protist Trypanosoma brucei
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Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET
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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Microbiology

Background:

  • MukBEF is a bacterial SMC (structural maintenance of chromosome)-like protein complex.
  • It is proposed to function similarly to yeast condensin and cohesin in DNA compaction via loop extrusion.
  • The regulation of MukBEF's ATPase activity by its subunits and interacting proteins is not fully understood.

Purpose of the Study:

  • To investigate the MukBEF ATPase activity.
  • To identify inter- and intra-subunit interactions regulating this activity.
  • To elucidate the roles of specific interactions in DNA condensation and cell viability.

Main Methods:

  • Protein-protein crosslinking
  • Site-specific mutagenesis
  • ATPase activity assays

Main Results:

  • Interactions between the MukB hinge and neck regions are essential for ATPase activity.
  • The ParC subunit of topoisomerase IV inhibits MukB ATPase by disrupting this interaction.
  • MukE-DNA interaction is vital for cell viability.
  • MukF interaction with the MukB neck is necessary for ATPase activity and viability.

Conclusions:

  • Specific intramolecular and intermolecular interactions within MukBEF are critical for its function.
  • Topoisomerase IV modulates MukBEF activity, impacting chromosome dynamics.
  • Understanding these interactions provides insights into bacterial chromosome organization and segregation.