The University of Tokyo · 농업·생명과학
다이스케 츠구마 교수의 연구실은 식물 세포의 물리적 파괴 없이도 효율적으로 단백질과 유전자를 추출할 수 있는 혁신적 화학적 라이시스 방법을 개발하며, 식물 분자생물학과 신호전달 메커니즘의 해부에 주력하고 있습니다. 특히 VIP1과 같은 전사인자와 칼슘 신호, 단백질 인산화 등 기계적 자극과 스트레스 반응을 조절하는 분자 네트워크를 중심으로 연구를 전개하고 있으며, 식물의 성장과 발달 조절 메커니즘을 규명하고자 합니다. 또한 식물에서 G-단백질과 같은 핵심 신호 분자의 상호작용 단백질을 규명함으로써 식물의 환경 적응 메커니즘을 밝히는 데 기여하고 있습니다.
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Abstract Background Protein extraction is a frequent procedure in biological research. For preparation of plant cell extracts, plant materials usually have to be ground and homogenized to physically break the robust cell wall, but this step is laborious and time-consuming when a large number of samples are handled at once. Results We developed a chemical method for lysing Arabidopsis cells without grinding. In this method, plants are boiled for just 10 minutes in a solution containing a Ca 2+ ch
Asparagus officinalis (garden asparagus) is a dioecious perennial crop. For agricultural production of A. officinalis, male plants have advantages over female plants. The dioecism of A. officinalis is determined by the single dominant masculinizing M locus, which is involved in tapetal cell development in stamens, but thus far no specific M locus genes have been identified. We re-analyzed previously published RNA-Seq data for the A. officinalis transcriptome, cloned some genes, and discovered th
VIP1 is a bZIP transcription factor in Arabidopsis (Arabidopsis thaliana). VIP1 transiently accumulates in the nucleus when cells are exposed to hypoosmotic conditions, but its physiological relevance is unclear. This is possibly because Arabidopsis has approximately 10 close homologs of VIP1 and they function redundantly. To examine their physiological roles, transgenic plants overexpressing a repression domain-fused form of VIP1 (VIP1-SRDXox plants), in which the gene activation mediated by VI
VIP1 and its close homologues can interact with calmodulins. Their nuclear-cytoplasmic shuttling requires neither MCA1 nor MCA2, but does require calcium signalling. Salt stress affects the VIP1-dependent regulation of root bending.
VIP1 is a bZIP transcription factor in Arabidopsis thaliana. When cells are exposed to mechanical stress, VIP1 transiently accumulates in the nucleus, where it regulates the expression of its target genes and suppresses mechanical stress-induced root waving. The nuclear-cytoplasmic shuttling of VIP1 is regulated by phosphorylation and calcium-dependent signaling, but specific regulators of these processes remain to be identified. Here, inhibitors of protein phosphatase 2A (PP2A) are shown to inh
Heterotrimeric G-proteins (G-proteins) have been implicated in ubiquitous signalling mechanisms in eukaryotes. In plants, G-proteins modulate hormonal and stress responses and regulate diverse developmental processes. However, the molecular mechanisms of their functions are largely unknown. A yeast two-hybrid screen was performed to identify interacting partners of the Arabidopsis G-protein β subunit AGB1. One of the identified AGB1-interacting proteins is the Arabidopsis adaptor protein AP-3µ.
VIP1 (VIRE2-INTERACTING PROTEIN 1) is a bZIP transcription factor in Arabidopsis thaliana. VIP1 and its close homologs (i.e., Arabidopsis group I bZIP proteins) are present in the cytoplasm under steady conditions, but are transiently localized to the nucleus when cells are exposed to hypo-osmotic conditions, which mimic mechanical stimuli such as touch. Recently we have reported that overexpression of a repression domain-fused form of VIP1 represses the expression of some touch-responsive genes
NDR/LATS-family protein kinases are conserved among eukaryotes. These protein kinases in yeast and animals phosphorylate specific targets and regulate the cell cycle. Arabidopsis thaliana has eight NDR/LATS-family protein kinase genes (NDR1-8), of which NDR2, NDR4, and NDR5 are involved in regulating pollen development. However, the functions of the other NDR/LATS-family protein kinase genes in plants are unclear. Here, we show that three putative phosphorylation sites of an Arabidopsis basic le
VirE2-INTERACTING PROTEIN1 (VIP1) is a basic leucine zipper protein in <i>Arabidopsis thaliana</i>. VIP1 changes its subcellular localization from the cytoplasm to the nucleus when cells are exposed to mechanical or hypo-osmotic stress. The nuclear localization of VIP1 is inhibited either by inhibitors of calcium signaling or by inhibitors of protein phosphatases 1, 2A and 4 (PP1, PP2A and PP4, respectively). VIP1 binds to the PP2A B"-family subunits, which have calcium-binding EF-hand motifs an
