Comparative analysis of two paradigm bacteriophytochromes reveals opposite functionalities in two-component signaling

Comparative analysis of two paradigm bacteriophytochromes reveals opposite functionalities in two-component signaling

The bacteriophytochrome DrBphP from Deinococcus radiodurans shows high sequence homology to the histidine kinase Agp1 from Agrobacterium fabrum but lacks kinase activity. Here, the authors structurally and biochemically analyse DrBphP and Agp1, showing that DrBphP is a light-activatable phosphatase.

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Detalles Bibliográficos
Autores principales: Elina Multamäki, Rahul Nanekar, Dmitry Morozov, Topias Lievonen, David Golonka, Weixiao Yuan Wahlgren, Brigitte Stucki-Buchli, Jari Rossi, Vesa P. Hytönen, Sebastian Westenhoff, Janne A. Ihalainen, Andreas Möglich, Heikki Takala
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2021
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Science
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Acceso en línea:https://doaj.org/article/769b0ce2dbfc4a7da26a63ec663601a0
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Sumario:The bacteriophytochrome DrBphP from Deinococcus radiodurans shows high sequence homology to the histidine kinase Agp1 from Agrobacterium fabrum but lacks kinase activity. Here, the authors structurally and biochemically analyse DrBphP and Agp1, showing that DrBphP is a light-activatable phosphatase.

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