Near-infrared optogenetic pair for protein regulation and spectral multiplexing

Taras A. Redchuk, Evgeniya S. Omelina, Konstantin G. Chernov, Vladislav V. Verkhusha

Research output: Contribution to journalArticle

51 Scopus citations

Abstract

Multifunctional optogenetic systems are in high demand for use in basic and biomedical research. Near-infrared-light-inducible binding of bacterial phytochrome BphP1 to its natural PpsR2 partner is beneficial for simultaneous use with blue-light-activatable tools. However, applications of the BphP1-PpsR2 pair are limited by the large size, multidomain structure and oligomeric behavior of PpsR2. Here, we engineered a single-domain BphP1 binding partner, Q-PAS1, which is three-fold smaller and lacks oligomerization. We exploited a helix-PAS fold of Q-PAS1 to develop several near-infrared-light-controllable transcription regulation systems, enabling either 40-fold activation or inhibition. The light-induced BphP1-Q-PAS1 interaction allowed modification of the chromatin epigenetic state. Multiplexing the BphP1-Q-PAS1 pair with a blue-light-activatable LOV-domain-based system demonstrated their negligible spectral crosstalk. By integrating the Q-PAS1 and LOV domains in a single optogenetic tool, we achieved tridirectional protein targeting, independently controlled by near-infrared and blue light, thus demonstrating the superiority of Q-PAS1 for spectral multiplexing and engineering of multicomponent systems.

Original languageEnglish (US)
Pages (from-to)633-639
Number of pages7
JournalNature Chemical Biology
Volume13
Issue number6
DOIs
StatePublished - Jun 1 2017

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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