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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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
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/769b0ce2dbfc4a7da26a63ec663601a0
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spelling	oai:doaj.org-article:769b0ce2dbfc4a7da26a63ec663601a02021-12-02T16:26:40ZComparative analysis of two paradigm bacteriophytochromes reveals opposite functionalities in two-component signaling10.1038/s41467-021-24676-72041-1723https://doaj.org/article/769b0ce2dbfc4a7da26a63ec663601a02021-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-24676-7https://doaj.org/toc/2041-1723The 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.Elina MultamäkiRahul NanekarDmitry MorozovTopias LievonenDavid GolonkaWeixiao Yuan WahlgrenBrigitte Stucki-BuchliJari RossiVesa P. HytönenSebastian WestenhoffJanne A. IhalainenAndreas MöglichHeikki TakalaNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-14 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q 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 Comparative analysis of two paradigm bacteriophytochromes reveals opposite functionalities in two-component signaling
description	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.
format	article
author	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
author_facet	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
author_sort	Elina Multamäki
title	Comparative analysis of two paradigm bacteriophytochromes reveals opposite functionalities in two-component signaling
title_short	Comparative analysis of two paradigm bacteriophytochromes reveals opposite functionalities in two-component signaling
title_full	Comparative analysis of two paradigm bacteriophytochromes reveals opposite functionalities in two-component signaling
title_fullStr	Comparative analysis of two paradigm bacteriophytochromes reveals opposite functionalities in two-component signaling
title_full_unstemmed	Comparative analysis of two paradigm bacteriophytochromes reveals opposite functionalities in two-component signaling
title_sort	comparative analysis of two paradigm bacteriophytochromes reveals opposite functionalities in two-component signaling
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/769b0ce2dbfc4a7da26a63ec663601a0
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Comparative analysis of two paradigm bacteriophytochromes reveals opposite functionalities in two-component signaling

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