Scientists have revealed new information on how red light-regulated histidine kinases function.
University of Jyväskylä - Jyväskylän yliopistoJun 14 2024 According to the study, altering of the length of a specific 'linker helix' region of the protein can even reverse their enzymatic activity. The study is published in Nature Communications.
Red light regulated histidine kinases Bacteria often sense and respond to their environment by applying receptor histidine kinase proteins. Once a histidine kinase senses an incident signal, it conveys this information to the cells by phosphorylating a response regulator protein. Bacterial phytochromes are red light sensing photoreceptors that usually function as histidine kinases.
Optogenetics aims to control cellular events with light, and bacterial phytochromes have traits that makes them especially good for this purpose. Due to this reason, we have previously generated an optogenetic pREDusk tool that is based on a bacterial phytochrome." Reversal of 'pREDusk' leads to 'pDERusk' An international collaboration between the groups of Dr. Heikki Takala from the University of Jyväskylä and Prof.
The process led to development of an inverted pREDusk tool that, unlike its predecessor, can activate bacterial gene expression under red light. "We named this new tool 'pDERusk'. This name first started as an unintended typo, but we noticed that would be a perfect name for an inverted 'pREDusk," Takala concludes.Journal reference:Meier, S. S. M., et al. . Leveraging the histidine kinase-phosphatase duality to sculpt two-component signaling. Nature Communications. doi.
Histidine Kinase Phosphatase Protein Research
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