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Red light-regulated interaction of Per-Arnt-Sim histidine kinases with partner histidine-containing phosphotransfer proteins in Physcomitrium patens.
Anami, Shu; Yamashino, Takafumi; Suzuki, Ryo; Nakai, Kota; Sato, Kensuke; Wu, Bowen; Ryo, Masashi; Sugita, Mamoru; Aoki, Setsuyuki.
Afiliación
  • Anami S; Graduate School of Informatics, Nagoya University, Nagoya, Japan.
  • Yamashino T; Graduate School of Bioagriculture, Nagoya University, Nagoya, Japan.
  • Suzuki R; Graduate School of Informatics, Nagoya University, Nagoya, Japan.
  • Nakai K; Graduate School of Informatics, Nagoya University, Nagoya, Japan.
  • Sato K; Graduate School of Informatics, Nagoya University, Nagoya, Japan.
  • Wu B; Graduate School of Informatics, Nagoya University, Nagoya, Japan.
  • Ryo M; Graduate School of Information Science, Nagoya University, Nagoya, Japan.
  • Sugita M; Graduate School of Informatics, Nagoya University, Nagoya, Japan.
  • Aoki S; Graduate School of Informatics, Nagoya University, Nagoya, Japan.
Genes Cells ; 26(9): 698-713, 2021 Sep.
Article en En | MEDLINE | ID: mdl-34086383
Multi-step phosphorelay (MSP) is a broadly distributed signaling system in organisms. In MSP, histidine kinases (HKs) receive various environmental signals and transmit them by autophosphorylation followed by phosphotransfer to partner histidine-containing phosphotransfer proteins (HPts). Previously, we reported that Per-Arnt-Sim (PAS) domain-containing HK1 (PHK1) and PHK2 of the moss Physcomitrium (Physcomitrella) patens repressed red light-induced protonema branching, a critical step in the moss life cycle. In plants, PHK homolog-encoding genes are conserved only in early-diverging lineages such as bryophytes and lycophytes. PHKs-mediated signaling machineries attract attention especially from an evolutionary viewpoint, but they remain uninvestigated. Here, we studied the P. patens PHKs focusing on their subcellular patterns of localization and interaction with HPts. Yeast two-hybrid analysis, a localization assay with a green fluorescent protein, and a bimolecular fluorescence complementation analysis together showed that PHKs are localized and interact with partner HPts mostly in the nucleus, as unprecedented features for plant HKs. Additionally, red light triggered the interactions between PHKs and HPts in the cytoplasm, and light co-repressed the expression of PHK1 and PHK2 as well as genes encoding their partner HPts. Our results emphasize the uniqueness of PHKs-mediated signaling machineries, and functional implications of this uniqueness are discussed.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Transducción de Señal / Bryopsida / Histidina Quinasa / Luz Idioma: En Revista: Genes Cells Asunto de la revista: BIOLOGIA MOLECULAR Año: 2021 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Reino Unido
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Transducción de Señal / Bryopsida / Histidina Quinasa / Luz Idioma: En Revista: Genes Cells Asunto de la revista: BIOLOGIA MOLECULAR Año: 2021 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Reino Unido