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Manisha,

Publications and source records attributed to Manisha,.

2 recordsLinked to original sources

Ancient intraflagellar transport machinery controls unique spatial distribution of phototropin in an evolutionary important non-flagellated vegetative stage of terrestrial alga

Intraflagellar transport (IFT) is a conserved trafficking system in eukaryotes that moves proteins along microtubules. It is best known for its essential role in building and maintaining cilia and flagella. Intriguingly, several IFT components are still found in organisms that no longer possess flagella, raising important questions about their original functions and how they may have been repurposed during evolution. The filamentous alga Klebsormidium nitens, positioned at the base of the streptophyte lineage, offers a valuable model for exploring this transition. Here, we investigate the IFT machinery in K. nitens and its relationship with the blue-light photoreceptor phototropin. Comparative genomic analyses show that key IFT-A and IFT-B components are retained, despite the complete loss of flagella in vegetative state. Cellular detection and immunofluorescence studies revealed the presence and localisation of IFT components, interestingly, their co-localization with phototropin. Notably, IFT-139 and IFT-20 strongly co-localize with phototropin at plasma membrane-associated regions. Phototropin overlapping localization (plasma membrane associated) with conserved phospho-adaptor protein 14-3-3, pointing to a phosphorylation-dependent signaling network. Unlike in Chlamydomonas reinhardtii, where these proteins localize to flagella, their interaction in K. nitens occurs independently of cilia presence. Together, these results evidenced that IFT components were retained and repurposed early in streptophyte evolution and might support phototropin localization and signalling, revealing an ancestral, non-ciliary role for the IFT system.

cell biology↗

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

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.

bioinformatics↗