ArticlebioRxiv : the preprint server for biology2025
The accessory protein CvnF8 modulates histidine kinase activity in an Actinobacterial G protein system in
Article in bioRxiv : the preprint server for biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Conservons are regulatory systems found in bacteria of the phylum Actinomycetota. These regulatory systems are composed of four core proteins: a sensor histidine kinase-like protein (CvnA homolog), an MglA-type roadblock protein (CvnB homolog), a protein containing a domain of unknown function (CvnC homolog), and small Ras-like GTPase (CvnD homolog). Based on their conserved small GTPase components and their phylogenetic distribution, we propose that conservons should be known as Actinobacterial G protein systems (AGPSs). The signal transduction path through AGPSs remains poorly understood, and some AGPSs have additional accessory proteins (CvnE and CvnF homologs) of unknown function. In this work, we show that AGPS accessory proteins are present when the cognate histidine kinase protein (CvnA homolog) lacks an extracytoplasmic sensory domain. It was previously shown that the Cvn8 AGPS of
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