Illuminating the inner workings of a natural protein switch: Blue-light sensing in LOV-activated diguanylate cyclases

Author:

Vide Uršula1ORCID,Kasapović Dženita1,Fuchs Maximilian1ORCID,Heimböck Martin P.1,Totaro Massimo G.1ORCID,Zenzmaier Elfriede1,Winkler Andreas12ORCID

Affiliation:

1. Institute of Biochemistry, Graz University of Technology, Petersgasse 12/II, 8010 Graz, Austria.

2. BioTechMed-Graz, Mozartgasse 12/II, 8010 Graz, Austria.

Abstract

Regulatory proteins play a crucial role in adaptation to environmental cues. Especially for lifestyle transitions, such as cell proliferation or apoptosis, switch-like characteristics are desirable. While nature frequently uses regulatory circuits to amplify or dampen signals, stand-alone protein switches are interesting for applications like biosensors, diagnostic tools, or optogenetics. However, such stand-alone systems frequently feature limited dynamic and operational ranges and suffer from slow response times. Here, we characterize a LOV-activated diguanylate cyclase (LadC) that offers precise temporal and spatial control of enzymatic activity with an exceptionally high dynamic range over four orders of magnitude. To establish this pronounced activation, the enzyme exhibits a two-stage activation process in which its activity is inhibited in the dark by caging its effector domains and stimulated upon illumination by the formation of an extended coiled-coil. These switch-like characteristics of the LadC system can be used to develop new optogenetic tools with tight regulation.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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