九州大学 研究者情報
論文一覧
寺本 岳大(てらもと たかまさ) データ更新日:2021.06.24

助教 /  農学研究院 生命機能科学部門 生物機能分子化学講座


原著論文
1. Teramoto T., Nishio T., Kurogi K. ,Sakakibara Y., Kakuta Y., The crystal structure of mouse SULT2A8 reveals the mechanism of 7α-hydroxyl, bile acid sulfation, Biochemical and Biophysical Research Communications, 2021.07.
2. Teramoto T., b,Kaitany K.J., Kakuta Y., Kimura M., Fierke C.A., Hall T.M.T., Pentatricopeptide repeats of protein-only RNase P use a distinct mode to recognize conserved bases and structural elements of pre-tRNA, Nucleic Acids Research, 10.1093/nar/gkaa627, 2020.12, Pentatricopeptide repeat (PPR) motifs are α-helical structures known for their modular recognition of single-stranded RNA sequences with each motif in a tandem array binding to a single nucleotide. Protein-only RNase P 1 (PRORP1) in Arabidopsis thaliana is an endoribonuclease that uses its PPR domain to recognize precursor tRNAs (pre-tRNAs) as it catalyzes removal of the 5′-leader sequence from pre-tRNAs with its NYN metallonuclease domain. To gain insight into the mechanism by which PRORP1 recognizes tRNA, we determined a crystal structure of the PPR domain in complex with yeast tRNAPhe at 2.85 Å resolution. The PPR domain of PRORP1 bound to the structurally conserved elbow of tRNA and recognized conserved structural features of tRNAs using mechanisms that are different from the established single-stranded RNA recognition mode of PPR motifs. The PRORP1 PPR domain-tRNAPhe structure revealed a conformational change of the PPR domain upon tRNA binding and moreover demonstrated the need for pronounced overall flexibility in the PRORP1 enzyme conformation for substrate recognition and catalysis. The PRORP1 PPR motifs have evolved strategies for protein-tRNA interaction analogous to tRNA recognition by the RNA component of ribonucleoprotein RNase P and other catalytic RNAs, indicating convergence on a common solution for tRNA substrate recognition..
3. Jun Zhang, Takamasa Teramoto, Chen Qiu, Robert N. Wine, Lauren E. Gonzalez, Susan J. Baserga, Traci M.T. Hall, Nop9 recognizes structured and single-stranded RNA elements of preribosomal RNA, RNA, 10.1261/rna.075416.120, 26, 8, 1049-1059, 2020.08.
4. Takuo Minato, Takamasa Teramoto, Yoshimitsu Kakuta, Seiji Ogo, Ki-Seok Yoon, Biochemical and structural characterization of a thermostable Dps protein with His-type ferroxidase centers and outer metal-binding sites, FEBS OPEN BIO, 10.1002/2211-5463.12837, 10, 7, 1219-1229, 2020.07.
5. Zakaria Omahdi, Yuto Horikawa, Masamichi Nagae, Kenji Toyonaga, Akihiro Imamura, Koichi Takato, Takamasa Teramoto, Hideharu Ishida, Yoshimitsu Kakuta, Sho Yamasaki, Structural insight into the recognition of pathogen-derived phosphoglycolipids by C-type lectin receptor DCAR, Journal of Biological Chemistry, 10.1074/jbc.RA120.012491, 295, 17, 5807-5817, 2020.04, [URL], The C-type lectin receptors (CLRs) form a family of pattern recognition receptors that recognize numerous pathogens, such as bacteria and fungi, and trigger innate immune responses. The extracellular carbohydrate-recognition domain (CRD) of CLRs forms a globular structure that can coordinate a Ca2+ ion, allowing receptor interactions with sugar-containing ligands. Although well-conserved, the CRD fold can also display differences that directly affect the specificity of the receptors for their ligands. Here, we report crystal structures at 1.8 -2.3 Å resolutions of the CRD of murine dendritic cell-immunoactivating receptor (DCAR, or Clec4b1), the CLR that binds phosphoglycolipids such as acylated phosphatidyl-myo-inositol mannosides (AcPIMs) of mycobacteria. Using mutagenesis analysis, we identified critical residues, Ala136 and Gln198, on the surface surrounding the ligand-binding site of DCAR, as well as an atypical Ca2+-binding motif (Glu-Pro-Ser/EPS168-170). By chemically synthesizing a water-soluble ligand analog, inositol-monophosphate dimannose (IPM2), we confirmed the direct interaction of DCAR with the polar moiety of AcPIMs by biolayer interferometry and co-crystallization approaches. We also observed a hydrophobic groove extending from the ligand-binding site that is in a suitable position to interact with the lipid portion of whole AcPIMs. These results suggest that the hydroxyl group-binding ability and hydrophobic groove of DCAR mediate its specific binding to pathogen-derived phosphoglycolipids such as mycobacterial AcPIMs..
6. Takuyu Hashiguchi, Katsuhisa Kurogi, Takehiko Shimohira, Takamasa Teramoto, Ming Cheh Liu, Masahito Suiko, Yoichi Sakakibara, Δ4-3-ketosteroids as a new class of substrates for the cytosolic sulfotransferases, Biochimica et Biophysica Acta - General Subjects, 10.1016/j.bbagen.2017.08.005, 1861, 11, 2883-2890, 2017.11, [URL], Cytosolic sulfotransferase (SULT)-mediated sulfation is generally known to involve the transfer of a sulfonate group from the active sulfate, 3′-phosphoadenosine 5′-phosphosulfate (PAPS), to a hydroxyl group or an amino group of a substrate compound. We report here that human SULT2A1, in addition to being able to sulfate dehydroepiandrosterone (DHEA) and other hydroxysteroids, could also catalyze the sulfation of Δ4-3-ketosteroids, which carry no hydroxyl groups in their chemical structure. Among a panel of Δ4-3-ketosteroids tested as substrates, 4-androstene-3,17-dione and progesterone were found to be sulfated by SULT2A1. Mass spectrometry analysis and structural modeling supported a reaction mechanism which involves the isomerization of Δ4-3-ketosteroids from the keto form to an enol form, prior to being subjected to sulfation. Results derived from this study suggested a potential role of SULT2A1 as a Δ4-3-ketosteroid sulfotransferase in steroid metabolism..
7. Joel V Tamayo, Takamasa Teramoto, Seema Chatterjee, Traci M Tanaka Hall, Elizabeth R Gavis, The Drosophila hnRNP F/H Homolog Glorund Uses Two Distinct RNA-Binding Modes to Diversify Target Recognition, Cell Reports, 10.1016/j.celrep.2017.03.022, 19, 1, 150-161, 2017.04, [URL], The Drosophila hnRNP F/H homolog, Glorund (Glo), regulates nanos mRNA translation by interacting with a structured UA-rich motif in the nanos 3' untranslated region. Glo regulates additional RNAs, however, and mammalian homologs bind G-tract sequences to regulate alternative splicing, suggesting that Glo also recognizes G-tract RNA. To gain insight into how Glo recognizes both structured UA-rich and G-tract RNAs, we used mutational analysis guided by crystal structures of Glo's RNA-binding domains and identified two discrete RNA-binding surfaces that allow Glo to recognize both RNA motifs. By engineering Glo variants that favor a single RNA-binding mode, we show that a subset of Glo's functions in vivo is mediated solely by the G-tract binding mode, whereas regulation of nanos requires both recognition modes. Our findings suggest a molecular mechanism for the evolution of dual RNA motif recognition in Glo that may be applied to understanding the functional diversity of other RNA-binding proteins..
8. Kathleen L McCann, Takamasa Teramoto, Jun Zhang, Traci M Tanaka Hall, Susan J Baserga, The molecular basis for ANE syndrome revealed by the large ribosomal subunit processome interactome, eLife, 10.7554/eLife.16381, 5, 2016.04, [URL], ANE syndrome is a ribosomopathy caused by a mutation in an RNA recognition motif of RBM28, a nucleolar protein conserved to yeast (Nop4). While patients with ANE syndrome have fewer mature ribosomes, it is unclear how this mutation disrupts ribosome assembly. Here we use yeast as a model system and show that the mutation confers growth and pre-rRNA processing defects. Recently, we found that Nop4 is a hub protein in the nucleolar large subunit (LSU) processome interactome. Here we demonstrate that the ANE syndrome mutation disrupts Nop4's hub function by abrogating several of Nop4's protein-protein interactions. Circular dichroism and NMR demonstrate that the ANE syndrome mutation in RRM3 of human RBM28 disrupts domain folding. We conclude that the ANE syndrome mutation generates defective protein folding which abrogates protein-protein interactions and causes faulty pre-LSU rRNA processing, thus revealing one aspect of the molecular basis of this human disease..
9. Takamasa Teramoto, Yukari Fujikawa, Yoshirou Kawaguchi, Katsuhisa Kurogi, Masayuki Soejima, Rumi Adachi, Yuichi Nakanishi, Emi Mishiro-Sato, Ming Cheh Liu, Yoichi Sakakibara, Masahito Suiko, Makoto Kimura, Yoshimitsu Kakuta, Crystal structure of human tyrosylprotein sulfotransferase-2 reveals the mechanism of protein tyrosine sulfation reaction, Nature communications, 10.1038/ncomms2593, 4, 2013.04, [URL], Post-translational protein modification by tyrosine sulfation has an important role in extracellular protein-protein interactions. The protein tyrosine sulfation reaction is catalysed by the Golgi enzyme called the tyrosylprotein sulfotransferase. To date, no crystal structure is available for tyrosylprotein sulfotransferase. Detailed mechanism of protein tyrosine sulfation reaction has thus remained unclear. Here we present the first crystal structure of the human tyrosylprotein sulfotransferase isoform 2 complexed with a substrate peptide (C4P5Y3) derived from complement C4 and 3′- phosphoadenosine-5′-phosphate at 1.9 Å resolution. Structural and complementary mutational analyses revealed the molecular basis for catalysis being an S N 2-like in-line displacement mechanism. Tyrosylprotein sulfotransferase isoform 2 appeared to recognize the C4 peptide in a deep cleft by using a short parallel β-sheet type interaction, and the bound C4P5Y3 forms an L-shaped structure. Surprisingly, the mode of substrate peptide recognition observed in the tyrosylprotein sulfotransferase isoform 2 structure resembles that observed for the receptor type tyrosine kinases..
10. Takamasa Teramoto, Rumi Adachi, Yoichi Sakakibara, Ming Cheh Liu, Masahito Suiko, Makoto Kimura, Yoshimitsu Kakuta, On the similar spatial arrangement of active site residues in PAPS-dependent and phenolic sulfate-utilizing sulfotransferases, FEBS Letters, 10.1016/j.febslet.2009.08.016, 583, 18, 3091-3094, 2009.09, [URL], Mammalian sulfotransferases (STs) utilize exclusively the sulfuryl group donor 3′-phosphoadenosine 5′-phosphosulfate (PAPS) to catalyze the sulfurylation reactions based on a sequential transfer mechanism. In contrast, the commensal intestinal bacterial arylsulfate sulfotransferases (ASSTs) do not use PAPS as the sulfuryl group donor, but instead catalyze sulfuryl transfer from phenolic sulfate to a phenol via a Ping-Pong mechanism. Interestingly, structural comparison revealed a similar spatial arrangement of the active site residues as well as the cognate substrates in mouse ST (mSULT1D1) and Escherichia coli CFT073 ASST, despite that their overall structures bear no discernible relationship. These observations suggest that the active sites of PAPS-dependent SULT1D1 and phenolic sulfate-utilizing ASST represent an example of convergent evolution..
11. Takamasa Teramoto, Yoichi Sakakibara, Ming Cheh Liu, Masahito Suiko, Makoto Kimura, Yoshimitsu Kakuta, Snapshot of a Michaelis complex in a sulfuryl transfer reaction
Crystal structure of a mouse sulfotransferase, mSULT1D1, complexed with donor substrate and accepter substrate, Biochemical and Biophysical Research Communications, 10.1016/j.bbrc.2009.03.146, 383, 1, 83-87, 2009.05, [URL], We report the crystal structure of mouse sulfotransferase, mSULT1D1, complexed with donor substrate 3′-phosphoadenosine 5′-phosphosulfate and accepter substrate p-nitrophenol. The structure is the first report of the native Michaelis complex of sulfotransferase. In the structure, three proposed catalytic residues (Lys48, Lys106, and His108) were in proper positions for engaging in the sulfuryl transfer reaction. The data strongly support that the sulfuryl transfer reaction proceeds through an SN2-like in-line displacement mechanism..
12. Takamasa Teramoto, Yoichi Sakakibara, Ming Cheh Liu, Masahito Suiko, Makoto Kimura, Yoshimitsu Kakuta, Structural basis for the broad range substrate specificity of a novel mouse cytosolic sulfotransferase-mSULT1D1, Biochemical and Biophysical Research Communications, 10.1016/j.bbrc.2008.12.013, 379, 1, 76-80, 2009.01, [URL], The mouse cytosolic sulfotransferase, mSULT1D1, catalyzes the sulfonation of a wide range of phenolic molecules including p-nitrophenol (pNP), α-naphthol (αNT), serotonin, as well as dopamine and its metabolites. To gain insight into the structural basis for its broad range substrate specificity, we solved two distinct ternary crystal structures of mSULT1D1, complexed with 3′-phosphoadenosine-5′-phosphate (PAP) plus pNP or PAP plus αNT. The structures revealed that the mSULT1D1 contains an L-shaped accepter-binding site which comprises 20 amino acid residues and four conserved water molecules. The shape of the accepter-binding site can be adjusted by conformational changes of two residues, Ile148 and Glu247, upon binding with respective substrates..
13. Takamasa Teramoto, Yoichi Sakakibara, Kanako Inada, Katsuhisa Kurogi, Ming Cheh Liu, Masahito Suiko, Makoto Kimura, Yoshimitsu Kakuta, Crystal structure of mSULT1D1, a mouse catecholamine sulfotransferase, FEBS Letters, 10.1016/j.febslet.2008.10.035, 582, 28, 3909-3914, 2008.11, [URL], In mammals, sulfonation as mediated by specific cytosolic sulfotransferases (SULTs) plays an important role in the homeostasis of dopamine and other catecholamines. To gain insight into the structural basis for dopamine recognition/binding, we determined the crystal structure of a mouse dopamine-sulfating SULT, mouse SULT1D1 (mSULT1D1). Data obtained indicated that mSULT1D1 comprises of a single α/β domain with a five-stranded parallel β-sheet. In contrast to the structure of the human SULT1A3 (hSULT1A3)-dopamine complex previously reported, molecular modeling and mutational analysis revealed that a water molecule plays a critical role in the recognition of the amine group of dopamine by mSULT1D1. These results imply differences in substrate binding between dopamine-sulfating SULTs from different species..
14. Ayami Matsushima, Takamasa Teramoto, Hiroyuki Okada, Xiaohui Liu, Takatoshi Tokunaga, Yoshimitsu Kakuta, Yasuyuki Shimohigashi, ERRγ tethers strongly bisphenol A and 4-α-cumylphenol in an induced-fit manner, Biochemical and Biophysical Research Communications, 10.1016/j.bbrc.2008.06.050, 373, 3, 408-413, 2008.08, [URL], A receptor-binding assay and X-ray crystal structure analysis demonstrated that the endocrine disruptor bisphenol A (BPA) strongly binds to human estrogen-related receptor γ (ERRγ). BPA is well anchored to the ligand-binding pocket, forming hydrogen bonds with its two phenol-hydroxyl groups. In this study, we found that 4-α-cumylphenol lacking one of its phenol-hydroxyl groups also binds to ERRγ very strongly. The 2.0 Å crystal structure of the 4-α-cumylphenol/ERRγ complex clearly revealed that ERRγ's Leu345-β-isopropyl plays a role in the tight binding of 4-α-cumylphenol and BPA, rotating in a back-and-forth induced-fit manner..
15. Ayami Matsushima, Yoshimitsu Kakuta, Takamasa Teramoto, Takumi Koshiba, Xiaohui Liu, Hiroyuki Okada, Takatoshi Tokunaga, Shun Ichiro Kawabata, Makoto Kimura, Yasuyuki Shimohigashi, Structural evidence for endocrine disruptor bisphenol A binding to human nuclear receptor ERRγ, Journal of biochemistry, 10.1093/jb/mvm158, 142, 4, 517-524, 2007.10, [URL], Many lines of evidence reveal that bisphenol A (BPA) functions at very low doses as an endocrine disruptor. The human estrogen-related receptor γ (ERRγ) behaves as a constitutive activator of transcription, although the endogenous ligand is unknown. We have recently demonstrated that BPA binds strongly to ERRγ (KD = 5.5 nM), but not to the estrogen receptor (ER). BPA preserves the ERRγ's basal constitutive activity, and protects the selective ER modulator 4-hydroxytamoxifen from its deactivation of ERRγ. In order to shed light on a molecular mechanism, we carried out the X-ray analysis of crystal structure of the ERRγ ligand-binding domain (LBD) complexed with BPA. BPA binds to the receptor cavity without changing any internal structures of the pocket of the ERRγ-LBD apo form. The hydrogen bonds of two phenol-hydroxyl groups, one with both Glu275 and Arg316, the other with Asn346, anchor BPA in the pocket, and surrounding hydrophobic bonds, especially with Tyr326, complete BPA's strong binding. Maintaining the 'activation helix' (helix 12) in an active conformation would as a result preserve receptor constitutive activity. Our results present the first evidence that the nuclear receptor forms complexes with the endocrine disruptor, providing detailed molecular insight into the interaction features..

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