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Related Concept Videos

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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Histone Modification02:32

Histone Modification

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The histone proteins have a flexible N-terminal tail extending out from the nucleosome. These histone tails are often subjected to post-translational modifications such as acetylation, methylation, phosphorylation, and ubiquitination. Particular combinations of these modifications form “histone codes” that influence the chromatin folding and tissue-specific gene expression.
Acetylation
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Caspase, a family of cysteine proteases, serve as effectors in apoptosis. The ced3 gene in C.elegans was first identified to be involved in apoptosis. This gene encodes the ced-3 caspase that is similar to the interleukin-1-beta converting enzyme or ICE in mammals. In addition to apoptosis, caspases also function in the inflammatory response. Inflammatory caspases are essential in activating pro-inflammatory cytokines that recruit immune cells and block the replication of pathogens inside...
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Common Ion Effect

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Compared with pure water, the solubility of an ionic compound is less in aqueous solutions containing a common ion (one also produced by dissolution of the ionic compound). This is an example of a phenomenon known as the common ion effect, which is a consequence of the law of mass action that may be explained using Le Châtelier’s principle. Consider the dissolution of silver iodide:
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Network Covalent Solids02:18

Network Covalent Solids

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Network covalent solids contain a three-dimensional network of covalently bonded atoms as found in the crystal structures of nonmetals like diamond, graphite, silicon, and some covalent compounds, such as silicon dioxide (sand) and silicon carbide (carborundum, the abrasive on sandpaper). Many minerals have networks of covalent bonds.
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Spreading of Chromatin Modifications02:25

Spreading of Chromatin Modifications

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The histone proteins in the nucleosomes are post-translationally modified (PTM) to increase or decrease access to DNA. The commonly observed PTMs are methylation, acetylation, phosphorylation, and ubiquitination of lysine amino acids in the histone H3 tail region. These histone modifications have specific meaning for the cell. Hence, they are called "histone code". The protein complex involved in histone modification is termed as "reader-writer" complex.
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Exploring Caspase Mutations and Post-Translational Modification by Molecular Modeling Approaches
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Modifications to a common phosphorylation network provide individualized control in caspases.

Melvin E Thomas1, Robert Grinshpon1, Paul Swartz1

  • 1From the Department of Molecular and Structural Biochemistry, North Carolina State University, Raleigh, North Carolina 27608 and.

The Journal of Biological Chemistry
|February 8, 2018
PubMed
Summary

Low levels of caspase-3 activity are crucial for development. Evolutionary changes in caspase-3

Keywords:
X-ray crystallographyallosteric regulationapoptosisbiophysicscaspasecomputational biologyfluorescencemolecular dynamicsprotein evolution

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Evolutionary Biology

Background:

  • Caspase-3 is essential for programmed cell death (apoptosis).
  • Low-level caspase-3 activity is also vital for normal development, including lymphoid proliferation and erythroid differentiation.
  • Post-translational modifications, like phosphorylation by p38-MAPK, regulate caspase-3 activity but the allosteric mechanism is unclear.

Purpose of the Study:

  • To elucidate the allosteric mechanism by which caspase-3 activity is reduced.
  • To define the interaction networks facilitating this mechanism through evolutionary and structural analysis.

Main Methods:

  • Phylogenetic analysis to trace evolutionary changes in caspase-3.
  • Structural studies to visualize the allosteric site and interaction networks.
  • Biophysical methods to assess enzyme activity and dimer stability.

Main Results:

  • Ser150, present in ancient caspases, evolved with apoptotic caspases and reduces activity at certain pH.
  • Thr152, a mammalian-specific modification, acts as a 'kill switch,' abolishing caspase-3 activity.
  • Changes in the modified loop propagate to the active site via connecting structural elements (helix and hydrophobic cluster).

Conclusions:

  • Evolutionary modifications at the caspase-3 allosteric site fine-tune enzyme activity.
  • Ser150 provides a general reduction in activity, while Thr152 offers a specific switch to abolish activity.
  • These mechanisms allow cells to modulate caspase-3 levels for both developmental processes and apoptosis.