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Related Concept Videos

Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
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The molecular orbital theory describes the distribution of electrons in molecules in a manner similar to the distribution of electrons in atomic orbitals. The region of space in which a valence electron in a molecule is likely to be found is called a molecular orbital. Mathematically, the linear combination of atomic orbitals (LCAO) generates molecular orbitals. Combinations of in-phase atomic orbital wave functions result in regions with a high probability of electron density, while...
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Cooperative Allosteric Transitions01:58

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In mechanical engineering, the stability of systems under various forces is critical for designing durable and efficient structures. One fundamental way to explore these concepts is by analyzing systems like two rods connected at a pivot point, O, with a torsional spring of spring constant k at the pivot point. This system is similar in appearance to a scissor jack used to change tires on a car. In this case, the arms of the linkage (equivalent to the rods in this system) are entirely vertical,...
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Identification of Protein Interacting Partners Using Tandem Affinity Purification
10:02

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Published on: February 25, 2012

Pleiotropy as a mechanism to stabilize cooperation.

Kevin R Foster1, Gad Shaulsky, Joan E Strassmann

  • 1Ecology and Evolution, Rice University, Houston, Texas 77005, USA. krfoster@rice.edu

Nature
|October 8, 2004
PubMed
Summary

Pleiotropy, where genes affect multiple traits, can surprisingly promote cooperation. In Dictyostelium discoideum, the dimA gene links stalk formation to spore inclusion, preventing cheating and stabilizing social evolution.

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Area of Science:

  • Evolutionary biology
  • Developmental biology
  • Social behavior

Background:

  • Pleiotropy, a common genetic phenomenon, often constrains adaptive evolution by linking traits.
  • Cooperation presents an evolutionary puzzle due to the potential for cheating and the associated costs.

Purpose of the Study:

  • To investigate the role of pleiotropy in the evolution of cooperation.
  • To examine the function of the dimA gene in the social amoeba Dictyostelium discoideum.

Main Methods:

  • Genetic analysis of the dimA gene in Dictyostelium discoideum.
  • Observation of cell differentiation and behavior in response to DIF-1 signaling.
  • Assessment of spore formation and cell fate in wild-type and mutant strains.

Main Results:

  • The dimA gene is essential for receiving DIF-1 signals, promoting prestalk cell differentiation.
  • Mutations in dimA lead to exclusion from spores, even when cells avoid stalk formation.
  • This pleiotropic effect links the cost of stalk formation to spore production, limiting cheating.

Conclusions:

  • Pleiotropy can stabilize cooperation by creating genetic links between cheating and personal costs.
  • The dimA gene in Dictyostelium discoideum exemplifies how pleiotropy can favor cooperative adaptations.
  • Understanding pleiotropic constraints is crucial for explaining the evolution of complex social behaviors.