.
l m
r
( -
r
186
43
4 : 03/9 5275
43 5
- 5
43
43
5
F 43
l m
w
A A (
A j t k
A ( j v k
t
h
yl l l l t l
t yl l º x l
↓ u t s yw l
u m
º m DNA RNA
l º s ATP º y
t m l y º N2y t s l
u º m m l
95%ºCO2 m lN2º 2.7%l3.5% tm
o p º u ux 93%ºH2 s ls
× y 7%l y 0.3% l º t t tm° l º
y º t m y tx °
t ºl y t m
y l t CO2y
m l x
y m
78% º y mN2 y
º m
º × s l1905
t m x º tl y
t y m ε ºl1909 7 2
× t 175 l550g x
m y1913 ε l ls tº
t m º ⇄
yl ⇄ y t
m
y t°
x °t º yx ys m ⇄ º y tu
m ºlo y º p s
m x t yl
º predisposition y tu y t (Soltis et
al. 1995; Werner et al. 2014)m m º 6000
t l 4000 mt t u yt u
x º l u º ux x
y 4000 xx yl α y ux
u º u ux
t l
º t
° yl t l l
t m l
Polygala paniculata y s
y m l
tu x t m
β x
m1987 3 l1992 3 l m1992 4
l1993 10 l2001 l2003
m2009 4 m
v
l º ⇄
l x m x l x
y s l ⇄y m ºl l
s m ºl 1% s 4000 y
t yl º u x s m
º ys l ℃
º u t ys m l
t l m ×
ºl y y w l º
s m l × ºl
t ys m ºl × l
l t m
× ºl °
m
× º l s o p
℃ m l
2.6-dimethoxy-p-benzoquinone(DMBQ)y t m l
y l y m × º
l ºl m ºl
l l ° tu º
m º ℃ x ⇄ s
yl ºs x t tm ° l l
º y l y s y m
ºl × x l
t ℃ m º y l l
s l t m l
℃ l y m ºl t
x °t tm
ºl x l
s YUCCA y mYUCCA º
w lYUCCA RNAi ×
y y y x m l YUCCA
l y m y y
y x l y
t y m
l y
m l y
m l
s y x m ℃ ºl
º ⇄ys m º l
l t º txl
m l ºl y y x w l
y ⇄ y m
x l º x l
tu t t m
y u xl u y
s xl x t tm
l m1996 3 l2001 3
l m2001 6 l2004 9
m l2006 8 l
l2016 m
n -+
d 2LU 4 1
f h h
q r
× B D y a ºlLD50y1 ng/mouse l
t l 100% m
lC- y pore-forming toxin s m
37gl l t x l ºa
etx x w m
q r
a etx mRNA l ELISA northern blot l
37g uy 25g 10 t m
lprimer extension l
-15/-14 TG y l overlap u 3° phased A-tracts
2° phased A-tractsy y x m
PAGE x l phased A-tracts DNA º y
Bent DNA t y m
l Bent DNAyetx °t m NanH
t l Bent DNA DNA
l× 13 m t
s l 2° Phased A-tracts l
y y x metx Bent DNAº
t y l 5° A-tract lBending º
l l t m
P02
t f
q r
C. perfringensºl t x t l H2 : CO2 = 1 :
1x m l º t
x l ºl Fdx y ⇄ s
m ºl t ° lC. perfringens 13
x lNADH l y
m
q r
t 5’- 3’- in-frame gene pXM
m
C. perfringens 13 l Cmr y
m ºlC. perfringens 13 º
tsuicide vector l Cmr ºl 5’- º3’-
l y m l0.5%
GAM × u l ×
m colony PCR m s 13
l lL- ldhL
ldhL ºC. perfringens 13 y mldhL
clostridial cellulosome f
q r
Clostridium ºl s
s m x l s y l
y AT-rich s l s m lClostridium ×
ºl s y ⇄ y t l º ⇄
tm l º t x t u 1
s lClostridium AT-rich l
y m l×
l y t m
º× l m
q r
C. acetobutylicum eglA l -×
s pCC13 T7 l pCC13-eglA m
T7 RNA y × mT7II
m lSDS-PAGE EglA l CMC
l t y x m l pXM
t b eglA lb
y m lC. cellulolyticum °t l
t m
P04
2, GNNA
f q r
Escherichia coli YggSº 5’ (PLP)
s l x l l ↓ n t m
x lYggSy wt x ⇄ t y m
lE. coliyggS y2-aminobutyrate (2-AB)l2-ketobutyrate (2-KB)l l
( -Glu-2-AB-Gly) y t m lPLP s 5’
(PNP) l (PN) s y t m l
yggS s PROSC yPN m
ºl (glyA) yggS y s
y m u lyggS °t º ys yl
lYggS º t tm ºglyA yggS
⇄ m
q r
glyAyggS l º s l y t
y x m wt GlyA º Ser tetrahydrofolate (THF) x Gly 5,10-metylene-tetrahydrofolate (5,10-mTHF) mglyAyggS
ºl 5,10-mTHF ⇄ ( l lMetl )
mglyA ºl5,10-mTHF º (GCV)
t lYggS GCV y m l3-
(serA) º 5,10-mTHF y GCV lGCV
YggS mserAyggS ºGly y l l
lMetl m x lYggSyGCV
t y m
c ) f
q r
( 38 1 ( 8MG O 8( i ( 8MG O ( L 64 )%+%(%0.
º 8 CA A D 9 8 1AE C AA8 CA A D D D x s l
( m nº
9 8 38 H38 t (
m º 38 y l m
q r
H38 , u l1 7 8 D A H
3A4 (, 0 1 7 8 D 8 A E 8 D 3A4 (, ,
l+ y 38 m
38 º H38 t m↓ º y c, Z4 l
↓ Q9 ºt /% s H38 º Z4 Q9 ,% m1 A H 38 º”
s yl ( 8( ” y m
l1 8 A E 8 D 38 º 8( s m l
38 t 8( l H38 (
y m
P06
f β
q r
Ruminiclostridium josui Clostridium josui
consolidated bioprocessing, CBP l x
º ℃ ⇄ys m ºlR. josui RjoI
x l ℃ m
q r
R. josui x HiTrap Heparin HP HiTrap Q HP
RjoI l m lRjoI ºAy GmetATC
s l ºA T GmetAhTC s l RjoIºDpnI
s y x m Clostridium perfringens pJIR751
pKKM801 m dam- x pKKM801 DNA t
l lR. josui m
, t R. josui cel48A
pKKM801 lR. josui lRjCel48AΔdocº
t y x m lR. josui / t l
℃ lR. josui ℃ m
A
M F a
Ruminiclostridium josui Fae1A CE1
CBM6 ( )
CBM6 )
CBM6 ITC CBM6
=1.4× =3.2× pNP- =2.4×
)
2
=1.9× 3
) )
CBM6 Native affinity PAGE
ITC
P08
B , 1 C 6 e
F F a
Clostridium beijerinckii
C. beijerinckii )
C. beijerinckii C. beijerinckii
C. beijerinckii Cbei_0664 DNA)
C. cellulovorans
engO E. coli-Clostridium pMTL500E engO
( C. beijerinckii
1 %CMC
) C.
beijerinckii C. beijerinckii
f q r
EngE º Clostridium cellulovoransy
s m º l l l 3° Surface
layer homology x w l
1 ° s m ºlEngE l
m
q r
EngE l n l TLC m l
CMC PASC º 2 3 ylAvicel º y
x m lEngEº t s x m
lglucomannan lichenanlβ-glucan lxylan
º x mlichenanlglucomannanlβ-glucan º
y lEngEº β-1,4 m t lCMC
m l y3 mg/mL
x l y y m l t °
x l l y2° ESS x
m lEngE º lESS x
y m
P10
Clostridium cellulovoranst GH44A
f q r
Clostridium cellulovorans x engGH44A y °
x m x N GH44 C
⇄ t m l
x t y x
m ºEngGH44A l x
m
q r
w m x y l
º yl
t m CMClAvicellPASClxylan t tl
m lAvicel PASC º
º x yl s CMC l3 4 m
xylan l4 m lEngGH44Aº
s y x m CMC
t ↓ º50 s l↓ pHy5 s y x m
, 3 C , 1 - l r Ra c BAn
1, e 1, mi a2, d N 3, p 1
1y r o, 2JBIC, 3s
streptothricin ST SF-2111B Ser methyl malonate
Ala O-acylpeptide
SF-2111B BAC
O-acylpeptide NRPS
orf 1197 orf 1198 NRPS
orf 1195 orf 1196 O-acylpeptide
BLAST Orf 1195 Orf 1196 S-adenosyl-L-methionine hydroxide
adenosyltransferase asparagine synthase O-acylpeptide
BAC
BAC LCMS orf 1195
SF-2111B O-acylpeptide
Orf 1195 O-acylpeptide orf
1196
P12
, 3 r Ra 2 3 , 1 JI C
nl
t h e mi a d N p
y r o s
streptothricin (ST) BD-12
glycine FemAB family
Orf11 Gly-tRNAGly C.
Maruyama et al., Appl. Environ. Microbiol., 82, 3640-3648, 2016
Orf11 BD-12
sba Sba18 Sba18
aminoacyl-tRNA aa-tRNA Gly-tRNAGly
aa-tRNA Gly-tRNAGly
Ala-tRNAAla Ser-tRNASer Sba18 aa-tRNAaa
tRNA Sba18 tRNAaa
E. coli 3 tRNAGly 2 tRNAAla S. lividans tRNAGly
4 9 aa-tRNA Sba18
Sba18 tRNA in vitro
tRNA Sba18
SF-2111B
BD-12
GH134 ( β-1,4- 2 , ) ,
β- (Glycoside Hydrolase family 5 (GH5) GH26
) β- (Man134A) GH134 family
(Shimizu et al. J. Biol. Chem. 2015) Man134A
GH134
Man134A Man134A
β- Man134A (Man134A-E61A)
GH134 β- Man134A GH5 β-
Man5C Pichia pastoris pH
Man134A Man5C β-
β- Man134A
9 Man134A-E61A β-
E61 61 1
Man134A-E61A β- β-
Man134A-E61A
Man134A β-
P14
, 31 (
Fusarium graminearum
AreAp
AreAp AreAp
AreAp
F. graminearum JCM 9873 HP1 hep1 Tri6 TEF
Tef6 Ext
pH 3.5 2-3 pH
36 36
pH - 36 72
HPLC AreAp L-Thr L-Phe
AreAp L-Gln L-Gln L-Phe
L-Thr Tef6
Ext hep1 L-Thr
F. graminearum rw 3 *
i hε h h h h h h
)h h h hβ
h h
q r
Fusarium graminearum º l NIV C-7 y
x x m x NIV ºC-8
tF. sporotrichioides lC-4
Tri13 C-8 Tri1 y
y t m ºF. graminearum FgTRI13 x lNIV
y u x x m
q r
Tri5 w C-7, C-8 FgTri1
F. graminearum t feeding lC-4 FgTRI13
mC-7 y C-8 y C-4 º
ylC-7 ºC-8 x y C-4 º
l º s m lF. sporotrichioides FsTri13 FgTri13
C-8 Tri16 t feeding ylC-7
C-8 y C-4 º x x m
lFgTRI13 ºFsTRI13 lC-7 y x° C-8
y t x y t y mC-4 y
ºFgTRI1 º t x lNIV ºC-7 lC-8 y
C-4 y t u m
P16
s rw
f ( ) β
( )
q r
Fusarium graminearum º x m nº F.
graminearum (Thr)
y t m l Thr
y yl t º s m º
x l m
q r
w Thr wt y RT-PCR
l
y mF. graminearumº 3
ylThr º1 s
m lThr y
t m Thr l
y x Thr y
t y m lThr y
l t m
Aspergillus nidulans poly (ADP-ribose) glycohydrolase u f
q r
(ADP- ) (PAR) º s
º PAR poly (ADP-ribose) polymerase (PARP) poly (ADP-ribose)
glycohydrolase (PARG) y y t PARPº
DNA t t
Aspergillus nidulans parp ortholog y 1 ° y w A.
nidulans º parg ortholog º t º
parg x
q r
A. nidulans x parg 7
PARG 1 Mg2+ PAR PAR
LC-MS/MS ADP- y x
fungal PARG (fPARG)
Δfparg DNA DNA
fPARG º t
x º fPARG y PARG t y
P18
t
f ( )
( )
q r
º x
w s º t
x y °t º t t Coprinopsis
cinerea º y t y x
t t º C. cinerea
(HP) y °t
q r
t HP ×
t y C. cinerea º y t
y t x HP º “
t y
HP
HP º t º GlcNAc
s GlcNAc x x HP º
x t y
8PY 1YW
f β
q r
ºlATP l ⇄
s m l º
m l y wt l l y
⇄ yl y °t t tm l
ºl l
tl lHis-Asp HysA y
⇄ s m º HysA l
y ⇄ s x m
q r
lMito Tracker Red t ATP
x lHysA º y t m
ROS °t l ROS
Mito Sox Red t l l ROS
m º t yl
º mHysA ºl I Alternative factors s AifA, NdeA
y PCR x m l
yROS mHysA s lHis-Asp
⇄ °t m
P20
FSU
f h h (h )h
h( )
q r
º l DNA l mGenomic
SELEX-Seq(gSELEX-Seq)ºl x
in vitro s m ºl gSELEX-Seq
t XlnR lXlnR
m
q r
l XlnR t gSELEX 3
× m DNA l
lXlnR s GGCT(A/G)Ay m
lXlnR y m
DEGs 75 l51
y m lx°
ºXlnR s m lXlnR y
BLI t tl XlnR
m
f β q r
ºl x Membrane vesicles (MVs)
t m MVs l
y m l x MV wt
º ys l yMVs º y tm
ºlMV y t Buttiauxella agerstis CUETM77-167 l
MV m
q r
B. agrestis CUETM77-167 MVs FM4-64 t l 30
˚C 30 m MVs t l
MV m CUETM77-167
l MV l m l
TolB l MV
y 1.7 m tolB MV t wt ºltolB
MV 3.7 m
ºMVs TolBy t y mTolBº
t x ltolB º y y
l yMVs t m
l MVs y m
P22
rw
f ( ) * * + (
( + ( ) * + 2 3 :3
q r
t º °t
y w t
w °t º y t t
º º ys º
t y x ux
q r
º Pseudomonas putida KT2440 s SMDBS º
P. stutzeri t º pBP136::gfp pCAR1::gfp t º
t t
º 101~104 tº
y P. putida SMDBS(pBP136::gfp)
t t
°t 16S rRNA
y ty
y
t MP ULYY z
( (
q r
º t t º
º fitness y
n IncP-1 pBP136::gfp IncP-7 pCAR1::gfp °t
Pseudomonas putida KT2440 s PpY101 º
fitness y t 2° °t PpY101
º prophage1 kguKE y t y
º KT2440 ° fitnessy
u x
q r
KT2440 PpY101 pBP136::gfp pCAR1::gfp °t
u LB
competitive index
(CI) fitness KT2440 fitnessº t
PpY101 º KT2440 P1 prophage1
KT2440 kguKE KT2440 P1 kguKE 3°
°t pBP136::gfp pCAR1::gfp ° fitness
pBP136::gfp 3° fitnessy x pCAR1::gfp
KT2440 KT2440 P1 KT2440 kguKE fitnessy y KT2440 P1
kguKE ºfitness º prophage1 kguKE º pCAR1::gfp
fitness y y
P24
rw f
q r
º u
s º x t
w º t y
w º y w y t y s
º
q r
(CAR) pCAR1::rfp Km
Pseudomonas putida SM1443 P.putida KT2440 t
1.0 g 1.0 mL 250 mg/L u CAR
106 CFU/mL u (10 rpm) 48 h
30 C 48 h CAR GC-FID MPN
ºCAR y 40 s 10-12
y ºCARº s 10-12
y º x
x º x y CAR y
o rw
f ( ( ( (
q r
º w
° y t
ys º s t
y t tu x y t tu ys nº Rhodococcus
erythropolis 2 t 15g A
º A
q r
300 g 200 g W 332 ml 15g
1 Rhodococcus erythropolis 2 1.0
108cells/g-soil u A 2500mg/kg 15g 6
t A w A º
GC-FID t º 1/3 LB
A º6 96% y
º12 xx y t s y
º x y t y
tu y
P26
f ( ( ) )
( )
q r
y
t x º y w w
° t x º s
º
y u x
q r
º (UASB) t
UASB º n
ºCH4
60~70% CO2 9~17% º 100% º x
t º
t
t ty
º y t y
ty
º y t y
rw
f ( ( ( (
β
(
q r
° γ ys γ º 1
1
° s w º x t
t n w y
y γ º t
º γ w
q r
γ w x 0 2 5
γ º MRS wt 0
º5.8 107 cfu/g s 5 º2.6 108 cfu/g 16S
rRNA t 0 wt ºStaphylococcus y
40 % s y y ° Lactococcus y
5 º 90%y 5 ºLactobacillus y
x º 5 º y
y y ° Lactococcus x Lactobacillus y
P28
j zk j k
f ² ² ( ( β ( ) )
* *
( ) *
q r
o pº ° n º
y º y
° uxt º °
y
º ℃ o
p o p x
t º o p º °t
t o p o p
q r
600 x 22 Saccharomyces cerevisiae x
w 4 1 4
THI7 ZAP1 PXL1 GLG1 YRR1
GY-115 y uxt s GY-115 º
s 4- 4-VG x GY-115
10 kg GY-115 º °
10.2ºC x 14.9 2.27
y
w p
f ( Bayanjargal Sandagdorj(
(
q r
º γ s yIFN- w IL-10
IFN- y x º
y t x w
y y º w
u
q r
3 7 14 21 28
°t pH t pH
pH y x y
y
16S rRNA MiSeq L. curvatus
L. plantarumy y ×
IFN- w IL-10 IFN- w IL-10
y y y
t qPCR t
º L. curvatus º L.
plantarum L. brevis s y
P30
Isolation and Identification of Indigenous Yeast Fermenting Ethanol from Vegetable and Fruit Wastes
Fannisa Putri
1, 2, Makiko Sakka
1, Naoto Isono
1, Emi Kunitake
1, Tetsuya Kimura
1, Kazuo Sakka
1, Sunardi
2and Yuli Astuti Hidayat
2(
1Grad Sch Bioresources, Mie Univ,
2
Dept Environ Sci, Postgrad Sch Univ Padjadjaran, Indonesia)
The acceptance of vegetables and fruits each day in Bandung City, Indonesia, from various regions reaches hundreds of tons and produces a lot of organic wastes. In addition to the approach of waste product, recycling of vegetable and fruit wastes can be pursued through the concept of waste to energy. Vegetable and fruit wastes have the biological and chemical potential to produce bioethanol.
Biological potency owned by indigenous microorganisms was examined for fermentation of the
vegetable and fruit wastes. Among 8 yeast strains isolated from the wastes, 2 indigenous yeast strains
S1.2 and S2.2 showed an excellent ability of ethanol fermentation while 6 other yeasts did not show a
good result on this experiment. Strains S1.2 and S2.2 could ferment glucose in the medium consisting
of 20% glucose, 1% peptone and 0.5% yeast extract to accumulate ethanol about 9.5 to 10% in the
medium, indicating high ethanol recovery close to theoretical value. They grow best on 25-30 °C in
pH 3-6 and are capable of fermenting various monosaccharides such as glucose, xylose, mannose,
galactose, fructose, and arabinose to produce ethanol. Physiological properties and PCR-based 18S
rRNA gene sequences showed that strain S1.2 was closely related to
Hanseniaspora opuntiae andstrain S2.2, Pichia fermentans.
u yz 76 o i
q r
º l l m l
l y y t m º
lGFP l w
m
q r
ºSaccharomyces cerevisiae BY4741 lw GFP Yeast
GFP Clone Collection ThermoFisherScience m º YPD l
l l t mGFP
ºl ºROX3 YBL093C l ºNIC96 YFR002W l ºPHO86
YJL117W l ºSEC7 YDR170C m
l 50 MPal100 MPal150 MPal200 MPa 30 l
m l
m
50 MPa º º º x m100 MPa ºl
l y m150MPa y m200 MPa º
y m l l
s y100MPa y m ºl
l t m
P32
o
f β
q r
wt º ºs y ( 50g 10-20 ) ”
( 40-41g ) ” º
y y ” º y
⇄ s y t y y t ”
q r
” y y º
t y ESCRT º x
º y t ys
y x ” º y y
u º t y
.
f ( (
(
º 8 y 8-Hydroxydaidzein (1) 1)l
8-Hydroxyglycitein (2) 2)l8-Hydroxygenistein (3) 1) ys m l yl
Genistein Daidzein l l l
t m ºl x 1,2,3 HPLC
lTLC lHPLC l1H-NMR 99 l
y l
m
1) Hideo Esaki et al., Biosci. Biotechnol. Biochem., 62(4), 740-746 (1998).
Akira Hirota et al., Biosci. Biotechnol. Biochem., 68(6), 1372-1374 (2004).
P34
f h h h h
º l y
t m º l l w l
l l n t m
l º ⇄ t w l
t l ⇄ s l
n u ys m
º t y ⇄ s l y
t m
º y t yl º
t l m
ºTLClHPLC NMR mHPLC wt º tUV
y t l * t m l
C10:0x C30:0 99.5
m l kg y m
* , , FOOD Style 21, 17(3), 87-89(2013).
, , , , LONMSTP 7 R P(H26.10.30).
O
O
OH OH
HO O
O
OH OH
HO O
O
OH OH
HO
H3CO
OH
8-Hydroxydaidzein (1) 8-Hydroxyglycitein (2) 8-Hydroxygenistein (3)
1 2 4 3 6 5
7 8
P35
f ( ) * ( (
h( h) h*
q r
nº t m2017
( ) wt l x l t
A(1) m y
t y x m l B(2)
m
q r
(Vigna angularis, × ) l m
Toyopearl HW-40Cw ODS l24 kg
x 4.6 mg 1 l2.4 mg 2 mNMR w CD x 2º1
l1 s y x m l1 n pH 50% -
lUV/Vis m lpH 5
5 80% t m l l
t m
P36
Study on the color and stability of 3-O-substition of cyanidin
fAsmaa B. El-Meligy, 1,2 Takehiro Ishihara,1 Kin-ichi Oyama,3 Ahmed M. El-Nahas,2 Ahmed H. Mangood,2 and Kumi Yoshida1
(1 Graduate School of Informatics, Nagoya University, 2Faculty of Science, El-Menoufia University, Egypt,
2Research Institute for Materials Science, Nagoya University)
The purpose:
Anthocyanin natural dyes are important pigment that can be used as a food colorant, as well as a dye for dye sensitized solar cell. The main drawback is their instability; they are highly reactive by degrading under normal condition of storage. 3-O-glycosilation of anthocyanidin is considered to increase stability. To clarify this, we compared the stability of cyanidin (1) with 3-O-glucosylcyanidin (2) and 3-O-methylcyanidin (3). We also analyzed the effect of presence of co-pigments on the color and stability of pigment.
Method and Result:
2 was isolated from black soy bean (Glycine max). 1 was obtained by acidic hydrolysis of 2. 3 was synthesized from rutin (4). After tetra-benzylation of 4, sugar moiety was hydrolyzed, then 3-OH was methylated with CH3I.
After removal of Bn-protection group, our transformation method using Zn-reduction followed with air oxidation to be obtained 3. 1-3 were dissolved in aq. buffer solution of pH 1 and the stability of the solutions were investigated by recording UV-Vis Spectra. The results reveal that the 3-O-glycoside substitution of anthocyanin is the most stable followed by 3-methylation while the 3-hydroxyl is the least stable. Thus, 3-O-substition plays a role in retarding decomposition of anthocyanin. Addition of co-pigment, flavocommelin (5, 1-10 eq. to each pigment) gave increase in stability with bathochromic effect even in strong acidic condition.
f q r
(TTX)ºl Na+ s l l
y t m lTTX º t l
º s m l ºl (Cynops
ensicauda popei)x Cep-212w Cep-210 m x l °
ºlTTX y t m x l Cep º x
s l ℃ y s m ºl w ℃
l m
q r
l ℃ lCep-212
m l t ℃ w
t m l x Cep-210 s m
P38
T JVUPU
f (
(
q r
(+)-Muconin (1)º Rullinia mucosax s , α,β-
-γ- THF-THP , ° t . º,
℃ t, 1 u ,
.
q r
Acrolein (2) , Sharpless Sharpless
14 3 . t , 2 Pd t ℃
4 . (S)-(-)-glycidol (6) 3
7 . THF-THP 5 , γ-
9 , (+)-muconin (1) u s .
H O
2
C12H25 O OMOM
O
OH O
3
Cl2Pd(CH3CN)2 (10 mol%)
O O
C12H25 OMOM
4
8 OTBS
I OH
Pd, CO, base
THF OTBS O
O
9
O O
C12H25 OMOM
5 OH
HO O
6
O O
C12H25 O
14 steps
OPMB
7 O
3 steps
C H
O
( ) , h
1 ng a c l
proanthocyanidin
epigallocatechin oligomer
3
epigallocatechin tetramer (1)
2 4 3 3
3 7 8 9 6
epigallocatechin tetramer (1) 7 8 9
(1)
P40
Quinocidin 2 t E e p
io
Quinocidin Actinomyces sp. TP-A0019
3,4-dihydroquinolizinium Quinocidin
2-mercaptoethanol N-acetyl-L-cysteine Michael
Quinocidin cysteine
Quinocidin 1
1 3,5-lutidine 5 1 PBS (pH 7.4)
10 2-mercaptoethanol HPLC 2 1
2
1 Quinocidin Michael cysteine
1
P41
1 3 2 ,
A (PRM-A) (HIV)
HIV PRM-A HIV
PRM-A PRM-A
PRM-A PRM-A
(1-3) PRM-A
PRM-A 1 2, 3
4
P42
1 3 2 ,
(PRMs)
PRMs Man
PRMs
PRMs .
Candida albicans
PRMs Man
PRMs Man
PRMs Man
HO O
O HOHO
O HOHOHO OH
O O HOHOHO O HO O HOHO OH
HO O HOHO OH
O
O HOOO OH
O OH HOHO
HO
2PY UP XVWOLU S OVYWOVXH P H L ⁺ s TTLXLX
f q r
Pummerer º α
s m n t y yl Pummerer
º 2 x tm1)
l - º -
m lp-NO2DPPA º s l
t Pummerer y l x° -
y m lp-NO2DPPA x° Pummerer
- m
q r
n lp-NO2DPPA l DABCO t Pummerer y
l y y x m n
l t y m
l l º
l y y x m l α-
t Click tl m
References 1) (a) Shimada, K. et al. Tetrahedron Lett. 2000, 41, 4637. (b) Jiao, N. et al. Org. Lett. 2015, 17, 6186.
P44
○ q r
RBP CHOL °t º tm
ºlin vivo in vitro RBP CHOL m
q r
< 1> Wistar RBP CHOL l l
m lRBP in vitro CHOL m
< 2> RBP l tl
m< 3> RBP HiLoad 26/60 Superdex 200 pg
tlRBPF1 RBPF6 CHOL m lRBPF3 SOURCE 5RPC
ST 4.6/150 tl ° lCHOL
m l< 1> RBPº CHOL l
lCHOL l ° x
m< 2> RBP y lHypothetical protein OsJ_13801 (NCBI
accession no. EAZ29742l54.5KDa) m< 3> RBPF3º CHOL
mRBPF3A ºlRBPF3B RBPF3CºCHOL
lNon-specific lipid-transfer protein 1 (LTP1) (NCBI accession No.A2ZHF1l11.3KDa)
Lectin (NCBI accession No.Q01MB6l22.7KDa) x m
lRBPºin vivo ºl CHOLy
lin vitro ºl CHOL x l
Hypothetical protein OsJ_13801l CHOL
LTP1 Lectin m lRBP CHOL
m R S
Me
p-NO2DPPA (2.5 eq.) DABCO (2.5 eq.)
toluene, reflux, 2 h R S N3 O
20 examples up to 88% yield
alkyne
Cu+ (cat.) Bioactive Compounds
4 1
f ( ) (
( )
q r
º u y t m
ºl n y ⇄ s m ºl
y t m nºl DNA ODN
l ODN m
q r
× x t m º l
Lactobacillus rhamnosus GG ODN m96
ODN l48 s MHC
m lMHC ODN lmyoDN
myogenic ODN m
myoDNº” x l º℃ y m
lmyoDNºG ℃ y m
l ylmyoDN
m º º t x l º myoDN
l myoDN m l
º myoDN tl l
m
myoDN- ºl t l
l l y m
P46
4 1
f ( ( ( ( ) * ( )
( ) *
q r
º m nº l º
y t l s y t
m u l °
y y m nº l - 8EA7 8 D C AD D 88
5 2 N P5 yl × m ºlN P5
y x m
q r
( x l t m
N P5 l lN P5 +/ º
m l N P5 l+/
mN P5 ºl y t mN P5
R 4A lN P5 ºl .5
y % l .5 y )%/ l .5 y )%. l
. . (y %) t m x lN P5 º
y m nº lN P5
x
f ( ( ( ( (
(
[ ]
nº Achl10-8 mol/kg y SHR
w l t x m º
Ach lAch w ° y
w Ach m
[ ]
1lAch 11 SHR Ach Ach ºM3
1,1-Dimethl-4-diphenylacetoxypiperidinium 4-DAMP w Ach+4-DAMP l
10-8 mol/kg u l m
2l 15 SHR l º
m º m 1
l10-8 mol/kg Ach l m
3l SHR lAch10-8 mol/kg 30
l m
[ ]
ºl Ach l y
m l4-DAMP Ach y m
ºl t yl
m x Achº M3 l
l y l l y m
P48
f ( ( ( ( (
q r nº t (AcCh)y
(SHR) wt x AcChº
AcCh
AcChº w y 1,000 t
º AcCh SHR t w
q r γ º
t AcCh º u
LC-MS/MS MRM
t : 14 SHR
: 14 SHR º (n=6)
: 10 SHR 4
º (n=6) 1
q r t º γ y2.25 mg/g
y1.78 mg/g s º ºAcCh
s
º y
s º y
2( B
f (
q r
s B2 PCB2 º ―
― n ― y
t PCB2º ° x s y
y T °t º t t º PCB2
T x
q r
PCB2 PCB2 3-OG PCB2 3"-OG PCB2 3,3"-di-OG 25 µM × CD3 IFN- IL-17 º PCB2 3,3"-di-OG CD3
y IL-10 º x CD4
T wt PCB2 3,3"-di-OG IFN- IL-17 º y IL-10
º x IFN- s T-bet w IL-17
s ROR t T-bet ROR t ºPCB2 3,3"-di-OG
x PCB2 3,3"-di-OGºT T-betw ROR
t ― s IFN- IL-17 T
° y
P50
4 1 p 4 1
f ( (
(
q r
y
t nº ° s DNA y DNA
y t DNA º
t DNA DNA y
DNAy UHRF1y DNA methyltransferase 1
(DNMT1)y
DNMT1 DNA UHRF1y
DNA DNA y tu s º DNA
y DNA y tES (TKO) UHRF1 TKO
t DNA
q r
TKO DNA dCTP DNA
γ-H2AX (DNA
) × DNA º DNA
t UHRF1 y DNA
y DNA y
UHRF1 yDNA s
s CRISPR/Cas9 Uhrf1 TKO
u o f
( ( ) )
q r
y º x , .
º y t ys , º
t y . , w A. nidulans º
, y x t . º y
s wt t .
º, × , y x,
s º x, ,
º u x x .
q r
ε , y x , º pH1 3
, 50 % t . x , º t y x .
( ), º 5.0 102,103, 104
30 × , . GC-MS
x , º Ala, Val, w y t . ,
, º Bacteroides y
t . x , y y .
P52
4 1YW t t 4 1YW
f q r
D- y t y x
D-Ser º N- -D- NMDA
t D-Aspº t
D- y D- - DAO
y º D-Asp
y u x D-Asp y s x
D-Asp y x
q r
C57BL/6 × D-Asp ºL-Asp 4 D-Asp w
L-Asp DNA D-Asp
ºControl Asp L-Asp D-Asp º 2 D-Asp
º x L-Asp Prevotella
y º C57BL/6 ×
D-Asp Control D-Asp
º x y º D-Asp ⇄ º t y
P53
2 1 -
P
C pL
2 2 q A n o xM C
n aL n d L n C o mx
o o x m dM o p n
Lby o iRdM pL o o L
q o n Zx o n Rio iRxM
P
u d o n iL Nm
t ad L p
y nu ym dM o L p C o nmxns
p m R T y d M o L o
A DH A E I H A E9 G (3) o + L
o Qx L 9 o C nu i x L
o nu i x Qx L
A ( o m L n
x Lml m dM o L
Qx hZ ydMrdL o L L L L
n Zx o d L n Rip iR
d Lbo o p ym dM
P54
-2 D P
6 p n
x Q L L mlo m
n iRxM p 6 6 n L o t n
iRx Lbo n Rip e m xM p
x Rd m 6 o xM
P
o p ad L S n
xM o p -+ nux
dM o 6 L6 o d L n d 6 o
nm dMrd n Zx 6 L6 o n iL y n Sx Ri d Lbycyo yd p m iRdMrdL 1(
Ri RL6 q 6 o o dM-+ q
nux d L6 o p mx sd
nm dM
h hβ (h h (hi
h( h)
q r
º l
y l m º /
y l C8) °t ºl l l
s m t l
C D E D C8) y l nº
x m º
l m
q r
d l ls
m l C8) º t yl
º º m C2;6 w 4A BA 4ET0
m ºt º x yl y
m , l
y y t m º
s l m
P56
f q r
l º ⇄ t m l
(ER)x wt l × y x
m × ALG-2ºl ×
yl º x t tm
nºlALG-2 MISSLlMAP1B mMISSLº s ylMISSL lERx ERES ERGICl
y y x m l MAP1B yl ×
ALG-2 MISSL m ºlALG-2y
x lALG-2lMISSLlMAP1B w m
q r
ALG-2lMISSL l IMR-90 t
mALG-2lMISSL l y m
l s SEAP
HeLa t l mMISSLlALG-2 l
SEAP y 7 8 m
s lMISSLºALG-2 t
m lMAP1B SEAP lMISSLl
ALG-2 ylMAP1B m
x lALG-2lMISSLlMAP1B × l
y m
å 1 1 A t i
q r A11 (AnxA11)ºl
s l ×
s m l (ALS) l6° AnxA11
(G38R, D40G, G175R, G189E, R235Q, R346C)y w l ºl
Ca2+ °t l t m
q rHeLa SGFP2 AnxA11 (AnxA11-SGFP2) Ca2+
R-GECO1 l × s ionomycin
lAnxA11-SGFP2 Ca2+ m
q rAnxA11-SGFP2 t t ºlionomycin Ca2+ y x t m lAnxA11-SGFP2 ºl Ca2+ y t l lAnxA11-SGFP2 yl wt x l l
x mCa2+ AnxA11-SGFP2 º ys
x l x y t t y m
AnxA11 wt ºl l Ca2+ y t (G38R,
D40G, G189E) l [Ca2+]y n x t (G175R, R235Q, R346C)y m l °t ºlR235Q wt lCa2+
m x lAnxA11 t °x wt l ×
y m × yALS
t x tm
P58
1 2 3Hae f
q r
MAP1B º wt l
n y x t m nº ×
ALG-2 MAP1By mALG-2º ×
× n x lALG-2 MAP1B º
× t s m ALG-2
ABM-1 ABM-2 2°y t ylMAP1B º y
tm ºlMAP1B ALG-2 u lMAP1B
ALG-2 m
q r
MAP1B w ALG-2 lMAP1B n MAP1B
ALG-2 m lALG-2 MAP1B
1813-1848 36 m wt
MAP1B ALG-2 m lALG-2 ⇄
m Far-Western blotting MAP1B ALG-2 y
y x m x MAP1B ALG-2
m
ALG-2 MAP1B m ALG-2 º
MAP1B y y ºPocket 2y GF y m
. 33 - *(
s f
q r
acyl-ACP (Aas) thioesterase(‘TesA)
(FFA) . x Synechococcuselongatus PCC
7942x u FFA dAS1Tº 12L/12D 8L/16D º
y FFA x º
u º t s º dAS1T
s
q r
FFAy II PSII y
FFAy dAS1T º y º
(IM) FFA IM FFA
1) º IM dAS1T
t 8L/16D dAS1T y
x x °t FFA y
s y x PSII x
dAS1T ºWT Fv/Fmy IM y
° dAS1T º FFA PSIIy
y
1) Kato et al. Biotechnol. Biofuels. 10: 141. 2017.
P60
. 33- *( rw
f
q r º y t y,
º y w , y
y t . x , w º w ,
º s . , wt
CLD1 y . º, Synechococcus elongatus
PCC7942 w CLD1 s Synpcc7942_1028 ,
x s .
q r His-tag Synpcc7942_1028 (His6-1028) in vitro
, His6-1028 º t
y . x His6-1028 y ° y x
. His6-1028 S. elongatus PCC7942 (1028OX ) ,
. º (VC ) 1028OX º x y,
ºVC 1028OX y , yVC 60% t
. , , t s .
rw
f ( ( ) *
( ) *
q r
º u s l y m
º s x l
t ℃ tue x
t m x w º
t tm ºl Leptolyngbya boryana w
t ℃ l y
m
q r
mini-Tn5 pKUT-Tn5-Sm/Sp Escherichia colix L.
boryana l m l
SmR l u 13 °t SmR
m lt n SmR
y t y m y
s l 2,000 x
tl º m °t
m
P62
å
f ε h ( ( E 9 9BI
q r
Pentatricopeptide repeat PPR ºPPR °
RNA l wt RNA n
t m lin silico PPR yRNA
t y yl ºt s m ºl
RNA PPR t RNA x
t m
q r
RNA PpPPR_56º nad3 nad4 RNA ylnad3 RNA
u PPR PpPPR_56 m
PpPPR_56 t in vitro RNA l
nad3lnad4 RNA yl º nad3 RNA
t m x l nad3 nad4 RNA y
PpPPR_56 l PpPPR_56ºRNA
yl PpPPR_56º nad3lnad4 RNA RNA y x m
l PPR u lC PPR
yRNA y x m
1 å
f h (hε h( E 9 9BI
q r
s º º °yl
DNA º s m ºl RNA RNA
RNase o εRNA p
l RNA × ℃ m
q r
εRNA t RNA lRNA l
y x Pentatricopeptide repeat PPR m lRNase m t in vitro RNA
lNYN y1 RNA s m
l RNA u PPR NYN t l
εRNA m l εRNA
y x l εRNA l
RNA y x t m
P64
å
f ( ) * + ε ) ( β +
( ) * 9BI +
q r
ºl s m w
t l º HK x
m º HK °yl ºs
x t tm ºPAS Period-Arnt-Sim °2° HK PpHK3a PpHK3b
m
q r
PpHK3a PpHK3b t l mPAS ° HK
ºl x º °x x m l PAS ºl
º PAS s y mPpHK3a PpHK3b l
t l m
l y m l ×
l × y t m PCR l º
APB y t m y lPpHK3a
PpHK3bºlAPB º l t y x
m
rw - f
q r º )+ l
m wt l AA TI HP AITQPOTI AI ME PS º
⇄ y t mAA °
A;5 º AA AITQPOTI AI ME PS A5
º tyl y tm lA;5 º A5
t ylA;5 AA º t y
t m x lA;5 º AA ⇄ t y yl
°t º x t tm l º AA A;5
m
q r 1 G5 2 92 E 8E 1 l
A;5 1 - 1
CC CC CC m7MP ISLO
CLNI l l l E 8E 1 º CC CC
1 y yl1 - º1
y l s CC CC CC m x A;5 º1
⇄ s y x m 1 w A;5
l 9 t AA
4 l E 8E 1 º º
t yl1 - º y t s m x lA;5 º
l ⇄ s y m
P66
f h h h
q r
ºl wt ( )
( )y m ºl l
y l y m ° s
ºl l y
t yl º x t tm º
in vivo l
m s ºl u B ARR
l u m
q r
trans - zeatin 3 w t
m u
x LBD3 °t l s LBD4 m
lLBD3lLBD4 º
lLBD3lLBD4 º y x m
º y l t l
s y m ºlCYCD3;1lWOX4l
AINTEGUMENTA (ANT) t l y t l
25 p p AJ ,
1 y y S
. ,
. SA
. .
phy SA
phy phyAphyB SA NPR1
SA NPR1
SA NPR1
SA phyAphyB Pseudomonas syringae
SA BiFC phyB
NPR1 . phy NPR1 NPR1
SA
P68
3 5 h 4 3 25
, T
S
.
. .
,
, ,
.
, ,
Col-0 , , RT-qPCR
. ,
. .
, ,
, Col-0
Col(gl1) , , RNA-seq
. , Col-0
, Col(gl1) . . ,
, Col-0 Col gl1 Psm ES4326
, , Col-0 .
. .
I . A A C A C C C A
C A D D CAA C C D
AC C C . D A D C . C D ACC A 2 A
AD D C D C x 1 G CD A -A D C 1 - C
H y
Polar nuclear movement at the subcellular level is crucial during multiple events in eukaryotic development. In most cases, components and regulators of the cytoskeleton as well as nuclear envelope proteins are major components involved, as demonstrated by severe developmental disorders in respective mutants. In the Arabidopsis root epidermis, the nucleus initially assumes a position at the inner lateral membrane during cell elongation and moves towards the root hair after hair bulging. Except for its actin-dependence demonstrated by pharmacological studies, little is known about dynamic hallmarks and regulatory mechanisms underlying this polar nuclear migration.
Here, we report that nuclear auxin signaling and Rho-of-Plant (ROP) signaling direct actin-dependent polar nuclear migration towards the root hair bulge. Time-lapse imaging reveals that the nucleus located at the inner lateral membrane starts its actin-associated movement towards the outgrowing root hair in an ACTIN7 (ACT7)-dependent manner. Loss of ACT7 function as well as reduced or enhanced activation of ROP signaling alter polar nuclear migration. High auxin concentration or reduced CTR1 kinase function induce nuclear mis-positioning that is suppressed by ARF7 ARF19 loss of function, revealing that nuclear auxin signaling regulates nuclear migration. Our findings establish a mechanistic framework of auxin- and ROP-signaling-directed, ACT7-dependent polar nuclear migration in the Arabidopsis root epidermis.
P70
bdMh P Oik RTS r .-- NgoMpa
wtn fU vf mlV c
x Y ue s C A - D 1 G CD A ,I AC y
NR23
SRPP srpp
SRPP SRPP
5 SRPP
SRPP
2 SRPP
srpp SRPP
WT SRPP
srpp
t u y
f 1SP 6LX HUP( (
q r
H+-pyrophosphatase (H+-PPase) º (PPi) H+
2° °. PPiº s
. y
º s . H+-PPase (fugu5)
º w l w x
y t y(Plant Cell 2011, Frontiers Plant Sci. 2016)l l
MGRL fugu5ºlPPi t .
ºPPi .
q r
MGRL fugu5 º
y y y x .
y w t .
º × (NH4+) º .
PPi .
°x NH4+ ys . MGRL
w fugu5 º NH4+ PPi l º x
PPi H+-PPase º s t .
P72
f h h L YJOLX A LMHU (h h h h
) h( h)
q r
º ⇄ s . ,
s × w º , t ×
y . × º s ,
y . ,
s (Prunus persica)y × t y .
w × , ×
(BORs, NIPs) , .
q r
× , PpeBOR4y w ,
× y . , PpeBOR4 ,
PpeBOR4 , , × y
x . , × × l º ×
y x . , PME y ,
y t y PCR,
x x . , ×
℃ × y , PpeBOR4
t y .
1
90%
pap1-D Amethyst
19
6 (110 212 301 304 310 311) pap1-D
6 (212 225 301
304 305 310)
GFP 212
P74
Analysis of flavonoid content in Oenothera’s flower during senescence TEPPABUT Yada1, OYAMA Kin-ichi2, KONDO Tadao1, YOSHIDA Kumi1
(1Graduated School of Informatics, 2Research Institute for Materials Science, Nagoya University
Purpose
Flower of tsukimisou (Oenothera tetraptera) begins to bloom around 20:00 and fades in the morning.
The full-blooming flower is white, and then the color is changed to red during senescence. Other Oenothera flowers, such as komasuyoigusa (O. laciniata) and matsuyoigusa (O. stricta) also change the color from yellow to orange during senescence. Our research group is interested in this phenomenon of coloration, so the analysis of pigments in O. tetraptera’s petals was done.
Methods and Results
Petals of were collected at 0, 4, 7 and 12 hours after blooming and extracted with acidic condition (3% TFA in 50% acetonitrile). The extract was analyzed using 3D-detected HPLC with Develosil RPAQUEOUS-AR-3 reverse phase column. In the white petal extract, flavonol derivative was detected.
In the red petal extract, a peak of anthocyanin was observed with the flavonol. Using LC-MS analysis with authentic samples clarified that the flavonol was quercitrin with m/z = 449 [M+H]+, and anthocyanin was cyanidin 3-glucoside (Cy3G) with m/z = 449 [M]+. During senescence, the content of Cy3G increased, whereas the content of quercitrin was not changed. The same experiments were carried out using O. laciniata and O. stricta. In both flowers Cy3G was detected. The color change was clarified to be the de novo biosynthesis of Cy3G.
Y VTHNLU f
q r
º l t s m ºl
l t y x
t m nºl 45 stomagen
m l lstomagen 6
yl ⇄ s x m ºlstomagen ℃
lstomagen m
q r
ºlstomagen lstomagen y
t EPF2 m lEPF2
y mstomagen wt l
stomagen-CC ºlstomagen m ºl
stomagen ℃ ylEPF2 u ℃
t s t m lstomagen-CC l m
l l
w l l y
m ºlstomagen ℃ lstomagen
t m
http://www.amano-enzyme.co.jp/jp/
http://www.ichibiki.co.jp/
http://www.itoen.co.jp/
http://www.kantenpp.co.jp/
http://www.katokagaku.co.jp/
http://www.gifushellac.co.jp/
http://www.kirin.co.jp/
http://www.skk-net.com/
http://www.pasconet.co.jp/
http://www.shinsei-ip.ne.jp/
http://www.taiyokagaku.com/
http://www.tsuji-seiyu.co.jp/
http://www.tokaibsn.co.jp/
http://www.nakahyo.co.jp/
http://www.nippongene.com/
http://www.fnsugar.co.jp/
http://www.bfsci.co.jp/
http://www.pokkasapporo-fb.jp/
http://www.mizkan.co.jp/company/
http://www.yamamori.co.jp/
http://www.yomeishu.co.jp/
å
( r
)0 0 (- º
℃ ε
℃
Mizkan Holdings
℃
γ ε
β ℃ ε
+
℃ ε
ε
γ ε
β
β ℃ ( )
ε st
ε
℃ ε
℃
ε
ε ε
℃ γ
γ
ε
ε
β Δ β
,
γ ε
γ ε
β
θ ℃ ε
– ℃
γ ε
γ ε
ε ε
β ℃ ε
ε
℃
