Estimation of the available free energy in a LOV2-Jα photoswitch

Research output: Contribution to journalArticle

83 Citations (Scopus)

Abstract

Protein photosensors are versatile tools for studying ligand-regulated allostery and signaling. Fundamental to these processes is the amount of energy that can be provided by a photosensor to control downstream signaling events. Such regulation is exemplified by the phototropins - plant serine/threonine kinases that are activated by blue light via conserved LOV (light, oxygen and voltage) domains. The core photosensor of oat phototropin 1 is a LOV domain that interacts in a light-dependent fashion with an adjacent α-helix (Jα) to control kinase activity. We used solution NMR measurements to quantify the free energy of the LOV domain-Jα-helix binding equilibrium in the dark and lit states. These data indicate that light shifts this equilibrium by ∼3.8 kcal mol-1, thus quantifying the energy available through LOV-Jα for light-driven allosteric regulation. This study provides insight into the energetics of light sensing by phototropins and benchmark values for engineering photoswitchable systems based on the LOV-Jα interaction.

Original languageEnglish (US)
Pages (from-to)491-497
Number of pages7
JournalNature Chemical Biology
Volume4
Issue number8
DOIs
StatePublished - Aug 2008

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Light
Phototropins
Oxygen
Allosteric Regulation
Benchmarking
Protein-Serine-Threonine Kinases
Phosphotransferases
Ligands
Proteins

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology

Cite this

Estimation of the available free energy in a LOV2-Jα photoswitch. / Yao, Xiaolan; Rosen, Michael K.; Gardner, Kevin H.

In: Nature Chemical Biology, Vol. 4, No. 8, 08.2008, p. 491-497.

Research output: Contribution to journalArticle

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