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Chem Biol. 2012 Apr 20;19(4):507-17. doi: 10.1016/j.chembiol.2012.02.006.

Designing photoswitchable peptides using the AsLOV2 domain.

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1
Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, NC 27599, USA.

Erratum in

  • Chem Biol. 2012 Jul 27;19(7):926.

Abstract

Photocontrol of functional peptides is a powerful tool for spatial and temporal control of cell signaling events. We show that the genetically encoded light-sensitive LOV2 domain of Avena Sativa phototropin 1 (AsLOV2) can be used to reversibly photomodulate the affinity of peptides for their binding partners. Sequence analysis and molecular modeling were used to embed two peptides into the Jα helix of the AsLOV2 domain while maintaining AsLOV2 structure in the dark but allowing for binding to effector proteins when the Jα helix unfolds in the light. Caged versions of the ipaA and SsrA peptides, LOV-ipaA and LOV-SsrA, bind their targets with 49- and 8-fold enhanced affinity in the light, respectively. These switches can be used as general tools for light-dependent colocalization, which we demonstrate with photo-activable gene transcription in yeast.

Comment in

PMID:
22520757
PMCID:
PMC3334866
DOI:
10.1016/j.chembiol.2012.02.006
[Indexed for MEDLINE]
Free PMC Article
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