Hirano Y

References (5)

Title : Strigolactone perception and deactivation by a hydrolase receptor DWARF14 - Seto_2019_Nat.Commun_10_191
Author(s) : Seto Y , Yasui R , Kameoka H , Tamiru M , Cao M , Terauchi R , Sakurada A , Hirano R , Kisugi T , Hanada A , Umehara M , Seo E , Akiyama K , Burke J , Takeda-Kamiya N , Li W , Hirano Y , Hakoshima T , Mashiguchi K , Noel JP , Kyozuka J , Yamaguchi S
Ref : Nat Commun , 10 :191 , 2019
Abstract : The perception mechanism for the strigolactone (SL) class of plant hormones has been a subject of debate because their receptor, DWARF14 (D14), is an alpha/beta-hydrolase that can cleave SLs. Here we show via time-course analyses of SL binding and hydrolysis by Arabidopsis thaliana D14, that the level of uncleaved SL strongly correlates with the induction of the active signaling state. In addition, we show that an AtD14(D218A) catalytic mutant that lacks enzymatic activity is still able to complement the atd14 mutant phenotype in an SL-dependent manner. We conclude that the intact SL molecules trigger the D14 active signaling state, and we also describe that D14 deactivates bioactive SLs by the hydrolytic degradation after signal transmission. Together, these results reveal that D14 is a dual-functional receptor, responsible for both the perception and deactivation of bioactive SLs.
ESTHER : Seto_2019_Nat.Commun_10_191
PubMedSearch : Seto_2019_Nat.Commun_10_191
PubMedID: 30643123
Gene_locus related to this paper: arath-AtD14

Title : Structures of D14 and D14L in the strigolactone and karrikin signaling pathways - Kagiyama_2013_Genes.Cells_18_147
Author(s) : Kagiyama M , Hirano Y , Mori T , Kim SY , Kyozuka J , Seto Y , Yamaguchi S , Hakoshima T
Ref : Genes Cells , 18 :147 , 2013
Abstract : Strigolactones (SLs) are plant hormones that inhibit shoot branching. DWARF14 (D14) inhibits rice tillering and is an SL receptor candidate in the branching inhibition pathway, whereas the close homologue DWARF14-LIKE (D14L) participates in the signaling pathway of karrikins (KARs), which are derived from burnt vegetation as smoke stimulants of seed germination. We provide the first evidence for direct binding of the bioactive SL analogue GR24 to D14. Isothermal titration calorimetry measurements show a D14-GR24 binding affinity in the sub-micromolar range. Similarly, bioactive KAR1 directly binds D14L in the micromolar range. The crystal structure of rice D14 shows a compact alpha-/beta-fold hydrolase domain forming a deep ligand-binding pocket capable of accommodating GR24. Insertion of four alpha-helices between beta6 strand and alphaD helix forms the helical cap of the pocket, although the pocket is open to the solvent. The pocket contains the conserved catalytic triad Ser-His-Asp aligned with the oxyanion hole, suggesting hydrolase activity. Although these structural characteristics are conserved in D14L, the D14L pocket is smaller than that of D14. The KAR-insensitive mutation kai2-1 is located at the prominent long beta6-alphaD1 loop, which is characteristic in D14 and D14L, but not in related alpha-/beta-fold hydrolases.
ESTHER : Kagiyama_2013_Genes.Cells_18_147
PubMedSearch : Kagiyama_2013_Genes.Cells_18_147
PubMedID: 23301669
Gene_locus related to this paper: arath-KAI2.D14L , orysj-Q10QA5

Title : Differences in lipid distribution and expression of peroxisome proliferator-activated receptor gamma and lipoprotein lipase genes in torafugu and red seabream - Kaneko_2013_Gen.Comp.Endocrinol_184_51
Author(s) : Kaneko G , Yamada T , Han Y , Hirano Y , Khieokhajonkhet A , Shirakami H , Nagasaka R , Kondo H , Hirono I , Ushio H , Watabe S
Ref : General & Comparative Endocrinology , 184 :51 , 2013
Abstract : Lipid content is one of the major determinants of the meat quality in fish. However, the mechanisms underlying the species-specific distribution of lipid are still poorly understood. The present study was undertaken to investigate the mechanisms associated with lipid accumulation in two species of fish: torafugu (a puffer fish) and red seabream. The lipid content of liver and carcass were 67.0% and 0.8% for torafugu, respectively, and 8.8% and 7.3% for red seabream, respectively. Visceral adipose tissue was only apparent in the red seabream and accounted for 73.3% of its total lipid content. Oil red O staining confirmed this species-specific lipid distribution, and further demonstrated that the lipid in the skeletal muscle of the red seabream was mainly localized in the myosepta. We subsequently cloned cDNAs from torafugu encoding lipoprotein lipase 1 (LPL1) and LPL2, important enzymes for the uptake of lipids from blood circulation system into various tissues. The relative mRNA levels of peroxisome proliferator-activated receptor gamma (PPARgamma) and the LPLs of torafugu were determined by quantitative real-time PCR together with their counterparts in red seabream previously reported. The relative mRNA levels of PPARgamma and LPL1 correlated closely to the lipid distribution of both fish, being significantly higher in liver than skeletal muscle in torafugu, whereas the highest in the adipose tissue, followed by liver and skeletal muscle in red seabream. However, the relative mRNA levels of LPL2 were tenfold lower than LPL1 in both species and only correlated to lipid distribution in torafugu, suggesting that LPL2 has only a minor role in lipid accumulation. In situ hybridization revealed that the transcripts of LPL1 co-localized with lipids in the adipocytes located along the myosepta of the skeletal muscle of red seabream. These results suggest that the transcriptional regulation of PPARgamma and LPL1 is responsible for the species-specific lipid distribution of torafugu and red seabream.
ESTHER : Kaneko_2013_Gen.Comp.Endocrinol_184_51
PubMedSearch : Kaneko_2013_Gen.Comp.Endocrinol_184_51
PubMedID: 23337031
Gene_locus related to this paper: takru-h2rw43

Title : Gibberellin-induced DELLA recognition by the gibberellin receptor GID1 - Murase_2008_Nature_456_459
Author(s) : Murase K , Hirano Y , Sun TP , Hakoshima T
Ref : Nature , 456 :459 , 2008
Abstract : Gibberellins control a range of growth and developmental processes in higher plants and have been widely used in the agricultural industry. By binding to a nuclear receptor, GIBBERELLIN INSENSITIVE DWARF1 (GID1), gibberellins regulate gene expression by promoting degradation of the transcriptional regulator DELLA proteins, including GIBBERELLIN INSENSITIVE (GAI). The precise manner in which GID1 discriminates and becomes activated by bioactive gibberellins for specific binding to DELLA proteins remains unclear. Here we present the crystal structure of a ternary complex of Arabidopsis thaliana GID1A, a bioactive gibberellin and the amino-terminal DELLA domain of GAI. In this complex, GID1A occludes gibberellin in a deep binding pocket covered by its N-terminal helical switch region, which in turn interacts with the DELLA domain containing DELLA, VHYNP and LExLE motifs. Our results establish a structural model of a plant hormone receptor that is distinct from the mechanism of the hormone perception and effector recognition of the known auxin receptors.
ESTHER : Murase_2008_Nature_456_459
PubMedSearch : Murase_2008_Nature_456_459
PubMedID: 19037309
Gene_locus related to this paper: arath-GID1B

Title : Cloning, heterologous expression, renaturation, and characterization of a cold-adapted esterase with unique primary structure from a psychrotroph Pseudomonas sp. strain B11-1 - Suzuki_2003_Protein.Expr.Purif_30_171
Author(s) : Suzuki T , Nakayama T , Choo DW , Hirano Y , Kurihara T , Nishino T , Esaki N
Ref : Protein Expr Purif , 30 :171 , 2003
Abstract : A gene coding for an esterase (PsEst1, 1911bp in length) of the psychrotrophic bacterium Pseudomonas sp. B11-1 isolated from Alaskan soil was cloned and sequenced. The deduced amino acid sequence revealed a protein of 637 amino acid residues with a molecular mass of 69 kDa. Although the expression product, PsEst1, showed no appreciable sequence similarity (less than 15% identity) to any known proteins with the established biochemical functions, it is expected to be related to the alpha/beta hydrolase superfamily because it shared sequence motifs that have been identified with this superfamily. For example, a unique 'nucleophilic elbow' motif, -Gly(36)-Asp-Ser-Leu-Asn(40)-, was identified, and Ser(38) was predicted to constitute a catalytic triad with Asp(162) and His(303). PsEst1 was overexpressed using a T7 RNA polymerase transcription (pET21a) system in the Escherichia coli BL21(DE3) cells as an inclusion body. A soluble denatured form of the enzyme was purified to homogeneity in the presence of 8M urea, and the catalytically active form of the enzyme could be obtained by subsequent removal of urea by dialysis, where the addition of 0.1% Triton X-100 was essential for the efficient renaturation of the enzyme. To our knowledge, this was the first example of the successful renaturation of the recombinant cold-adapted enzyme. The enzyme efficiently hydrolyzed vinyl and aryl esters with the C4-C6 acyl chain. The activation energy of the enzymatic p-nitrophenyl butyrate hydrolysis (20.1 kcal/mol at 10 degrees C) was significantly lower than the value (79.9 kcal/mol) of the mesophilic lipase. It was observed that the K(m) values for p-nitrophenyl butyrate in the growth temperature range of strain B11-1 (5-15 degrees C) were lower than those at higher temperatures.
ESTHER : Suzuki_2003_Protein.Expr.Purif_30_171
PubMedSearch : Suzuki_2003_Protein.Expr.Purif_30_171
PubMedID: 12880765