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Related Concept Videos

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 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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Phosphorylation01:02

Phosphorylation

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The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...
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Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

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Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
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Energy to Drive Translocation01:37

Energy to Drive Translocation

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Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
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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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In Vitro Aggregation Assays Using Hyperphosphorylated Tau Protein
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ATP Kinetically Modulates Pathogenic Tau Fibrillations.

Chae Eun Heo1,2, Jong Yoon Han1,2, Sungsu Lim3

  • 1Department of Chemistry, Korea University, Seoul 02841, Republic of Korea.

ACS Chemical Neuroscience
|September 11, 2020
PubMed
Summary

Adenosine triphosphate (ATP) catalyzes tau protein fibrillation, a key process in Alzheimer's disease (AD). ATP acts as a catalyst, not a reactant, by attracting lysine residues to accelerate the formation of toxic tau aggregates.

Keywords:
Amyloid fibrillationamyloidogenic proteinsbiophysicsmass spectrometrysmall-angle X-ray scatteringtau

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Area of Science:

  • Neuroscience
  • Biochemistry
  • Molecular Biology

Background:

  • Tau aggregation is pathologically significant in Alzheimer's disease (AD) and tauopathies.
  • Understanding the molecular mechanisms driving tau aggregation is crucial for developing therapeutic strategies.

Purpose of the Study:

  • To investigate the role of adenosine triphosphate (ATP) in catalyzing tau protein fibrillation.
  • To elucidate the molecular interactions between ATP and tau protein during the aggregation process.

Main Methods:

  • Native mass spectrometry (MS)
  • Small-angle X-ray scattering (SAXS)
  • Molecular dynamics (MD) simulation
  • Biophysical characterization of tau protein (K18 domain) fibrillation.

Main Results:

  • ATP was found to catalyze the fibrillation of tau protein (K18) and human islet amyloid polypeptide.
  • ATP forms supramolecular complexes with lysine residues in tau's four-repeat domain, promoting dimer formation and accelerating fibril elongation.
  • ATP acts as a catalyst, not being incorporated into the final tau fibrils.
  • A correlation between ATP dyshomeostasis and tau aggregation in cellular environments was observed.

Conclusions:

  • ATP plays a catalytic role in tau fibrillation, offering a new perspective on AD pathogenesis.
  • The findings provide molecular-level insights into how ATP influences tau structure and aggregation.
  • Targeting ATP-tau interactions could be a potential therapeutic avenue for AD and related tauopathies.