Novel algal modular LOV domain proteins expand opto-biotechnological avenues for controlling of eukaryotic riboswitching, translational and proteolytic processes.

Abstract

Light, Oxygen, or Voltage (LOV) domains mediate blue light-gated signal transduction, regulating diverse opto-biological functions. LOV domain functions either standalone or fused with effector domains, regulating the downstream signalling process. The current repertoire of LOV domain-based tools is limited to a relatively small number of naturally occurring proteins. In this study, we have identified novel algal LOV domain fused with different effector domains as potential light-mediated translational, ribogenetic and proteolytic switches, highlighting their unexplored avenues of opto-biotechnology. LOV-domain fusion with eIF4E suggests its potential as a light-controlled translational switch and as an opto-ribogenetic regulator. LOV-SppA might be used as a light-gated proteolytic switch. Additionally, LOV coupled with UFD1, UbiH, mannosyl-oligosaccharide glucosidase and biosynthetic gene cluster (BCG) molecular chassis pave the way for opto-biomanufacturing strategies of relevant valuable algal bioactive. Here, we report the discovery of 13 novel algal modular LOV domain-containing proteins across the algal system through comprehensive bioinformatics, bio-curation and systems biology approaches. It offers important insights into the structural and functional diversity of LOV photoreceptors in algae. Hence, these newly identified modular LOV domain-containing proteins expand the platform of opto-biotechnology applications. These finding lay the foundation for future research on the mechanistic basis for light-driven signalling cascade of RNA, translational and protein homeostasis in algae, and potentiate development of next-generation opto-biotechnological tools for synthetic biology, optogenetics and opto-biomanufacturing of valuable bioactive via regulation of biosynthetic gene cluster (BGC) in green lineage.