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5 01. Pulse proteolysis [] pulse proteolysis Thermococcus kodakarensistk subtilisin Tk-RNase H2 Thermotoga maritimatm RNase H2 4 M GdnHCl GdnHCl pulse proteolysis [] GdnHCl Tk-subtilisin 45 s 8.5%(w/v) TCA 70%SDS-PAGE Tk-subtilisin SDS-PAGE Image J [] 4 M GdnHCl CD pulse proteolysis 3
6 02. 4
7 *03. Lactobacillus plantarum 22A-3 Jarukan Lamubol in vivo DSS Lactobacillus plantarum 22A-3 TGF-β1 mrna L. plantarum 22A-3 TGF-β1 in vitro Caco-2 RAW264.7 L. plantarum 22A cfu/ml LPS RAW264.7 TNF-α Killing Assay TGF-β1 ELISA Caco-2 RNA Real time PCR IL-8 mrna TGF-β1 mrna TGF-β1 RAW264.7 Recombinant Human TGF-β1 3 RAW264.7 TNF-α L. plantarum 22A-3 LPS TNF-α 53 41IL-8 mrna 80 Caco-2 TGF-β1 mrna TGF-β pg/ml 22A-3 Recombinant Human TGF-β1 RAW264.7 TNF-α L. plantarum 22A-3 Caco-2 TGF-β1 RAW264.7 TNF-α 5
8 *04. in vitro Caco-2 RBL-2H3RBL-2H3 DNP-IgE 6 DNP-albumin RBL-2H3 β-hexosaminidase Go6976 RBL-2H3 TNF-α killing assay RBL-2H3 Go6976 RBL-2H RBL-2H3 6
9 *05. SPS SPS(shoyu polysaccharides)(g- ) 1Balbc/A (5 ) 3 SPS G-SPS G- 5 (10 /) (25) 2 (n=7)(n=8) 2 1 (3mg)SPS(200mg)G- (100mg) SPS SPSG- G- SPSG- SPS G- 2 3 (6 ) 3 SPSG- 7
10 *06. mtorc1 PGC-1α 8
11 *07. Structural and functional analysis of bacterial cell-surface protein involved in alginate import Kanate Temtrirath, Kousaku Murata, and Wataru Hashimoto (Div. of Food Sci. Biotechnol., Grad. Sch. of Agric., Kyoto University) PurposeA Gram-negative bacterium, Sphingomonas sp. strain A1, inducibly forms a mouth-like pit on the cell surface in the presence of alginate polysaccharide. After accumulated on the cell surface, alginate is directly incorporated into the cytoplasm as a macromolecule via the pit called superchannel. Among cell-surface proteins involved in the formation of the pit and/or import of alginate, Algp7 (27 kda), a protein localized in the outer membrane, shows a capability to bind alginate, suggesting its contribution to accumulate alginate. Binding mode of alginate to Algp7, however, remains to be clarified. In the present study, structure and function relationship of Algp7 was analyzed. MethodsTertiary structure of Algp7 was determined by X-ray crystallography. A model for Algp7/alginate complex was constructed by docking simulation with a program of AutoDock. Binding affinity of wild-type Algp7 and its mutants with alginate was analyzed by UV absorption difference spectroscopy and differential scanning fluorimetry (DSF). Results and DiscussionCrystals of Algp7 formed in droplets containing alginate oligosaccharides were subjected to X-ray crystallography. Crystal structure of Algp7 was determined at a higher resolution (1.99 Å), although no oligosaccharides were included in the structure. Thus, docking simulation was carried out to investigate interaction between Algp7 and alginate. In silico model of Algp7/oligosaccharide was constructed by using atomic coordinates of Algp7 and oligosaccharides. In the model, some charged residues were found to be potential candidates for alginate binding. Subsequently, site-directed mutagenesis was carried out and four purified mutants, E79A, E194A, N221A, and K68A/K69A, were subjected to binding assay. The profile of UV absorption difference spectroscopy indicated that K68A/K69A exhibited a significant reduction (at least 20-fold decrease) in binding affinity with alginate compared with wild-type Algp7 (K d = M). Binding affinity of E79A, E194A, and N221A mutants with alginate was comparable with that of wild-type Algp7. This result was also supported by the DSF analysis. On the basis of these data, Lys68 and Lys69 residues of Algp7 probably play an important role in binding alginate. 9
12 *08. IRE1a α α β β α β α β α β α β α αβα β α β α 10
13 *09. MAPKKK18 ABA 11
14 *10. N- Mpr1 Saccharomyces cerevisiae N- Mpr1 Mpr1 ProArgArg Mpr1 Arg Arg Mpr1 Pro L P5C Mpr1 P5C L--γ- GSAArg N--GSA Mpr1 in vitro P5C/GSA Mpr1 ProArg Mpr1 Mpr1 Arg Mpr1 Mpr1Asn178Asp Arg Mpr1 Arg Mpr1 Mpr1 ProArg Mpr1 N- Arg Δarg5/6 Arg Mpr1 P5C/GSA Arg in vitro Mpr1 12
15 *11. Pichia pastoris Wsc Saccharomyces cerevisiae Wsc Wsc S. cerevisiae Wsc BLAST Pichia pastoris Wsc PpWSC1, PpWSC2, PpWSC3 3 Ppwsc1 Ppwsc1 3 Wsc Ppwsc1 PpWSC2 Ppwsc1Ppwsc2 Ppwsc1 PpWSC1 PpWSC2 13
16 *12. ABCG1 ABCG4 1 1, icems 14
17 *13. Rhodococcus erythropolis N9T-4 Rhodococcus erythropolis N9T- 4 CO 2 TEM X TEM-EDX 4,6-DAPI NR TBDAPI NR TB BM LB TB TB polyp polyp polyp - BM N9T-4 polyp TEM-EDX polyp 15
18 *14. Interaction of 8-Anilinonaphthalene 1-Sulfonate (ANS) and Thermolysin as Examined by ANS Fluorescence Vimbai Samukange, Masayuki Kamo, Kiyoshi Yasukawa, and Kuniyo Inouye (Div. of Food Sci. and Biotechnol., Grad. Sch. of Agric., Kyoto University) [Objective] Thermolysin is a thermostable neutral metalloproteinase produced in the culture broth of Bacillus thermoproteolyticus. It consists of 316 amino acid residues with one zinc ion required for enzyme activity and four calcium ions required for structural stability. Thermolysin activity increases with increasing concentrations of neutral salts in an exponential fashion. 1) ANS is a fluorescent probe. It emits a large fluorescence energy when the anilinonaphthalene group binds with proteins through hydrophobic interaction. The objective of this research is to examine the interaction of ANS and thermolysin. [Methods] Native thermolysin purified from B. thermoproteolyticus was used. Fluorescence spectra were measured with excitation at 380 nm and emission at nm for 25 µm ANS at 25 C. [Results] Without NaCl at ph 7.5, the fluorescence intensity at 490 nm (FI 490 ) increased by 20%, and the wavelength giving the maximum fluorescence (λ FImax ) decreased from 524 to 510 nm with increasing concentrations of thermolysin from 0 to 2.0 µm, suggesting that ANS binds thermolysin through hydrophobic interaction. With 1.0 µm thermolysin, FI 490 increased by 15%, and λ FImax decreased from 519 to 504 nm with increasing concentrations of NaCl from 0 to 4.5 M, suggesting that the interaction of ANS with thermolysin is enhanced by NaCl. 2) [References] 1. Inouye K, J. Biochem., 112, (1992). 2. Kamo M and Inouye K, Annual Meeting of JSBBA, p. 65 (2007). 16
19 *15. Sorgomol Sorgomol (1) Sorghum bicolor sorgomol (1) ethyl 2-oxocyclohexanecarboxylate 6 HPLC 1 2 HO O O 8 8a 8b 7 3 B C A 3a 4a 4 5 O Sorgomol (1) 9 3' 2' 1' O D 5' 4' 6' O 17
20 *16. ROS ROS 490 nm DCL DCL 8 DCL 8 Suzuki-Miyaura DCL 18
21 19
22 1. 2. ROSROS ROS 20
23 1 DCL DCL 13 C (100%) - 13 C DCL 13 C DCL DCL DCL DCL DCL DCL 390 DCL DCL 21
24 DCL DCL ROS 120 ROS DCL DCL DCL DTT DCL DTT 22
25 DCL DCL 120 DCL ROS ROS 23
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