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Ramani, S. and S.K. Apte 1997. Transient expression of multiple genes in salinity‐
stressed young seedlings of rice (Oryza sativa L.) cv. Bura Rata. Biochem. Biophys. Res.
Commun. 233:663‐667.
Yoshida, S., D. A. Forna, J. A. Cock and K. A. Gomez. 1976. Laboratory manual for
physiological studies of rice. International Rice Research Institute, Manila, Philippines. :
62.
平成15年度助成研究報告集Ⅰ(平成17年3月発行)
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a
ab
b
a
b
a
0 mM NaCl300 mM NaCl655 mM NaCl
Fig. 1. Leaf photosynthesis of wild Oryza species in differentNaCl conditions.Leaf photosynthesis estimated by oxygen evolution.0mM NaCl value of O. latifolia and O. rufipogon was 89and 78 µmolO2 mgChl-1 hr-1, respectively. Values representmean of three or four plants per treatment.Means followed by the same letters are not significantlydifferent at 5% of probability according to Fisher multiplerange test.
平成15年度助成研究報告集Ⅰ(平成17年3月発行)
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a
a
a
a
ab
b
0 mM NaCl300 mM NaCl655 mM NaCl
Fig. 2. O2 evolution rate of thylakoid membrane in wild Oryza species.Initial values of O.latifolia and O. rufipogon were 33 and 58µmolO2 mgChl-1 hr-1, respectively. Values represent mean of threeplants per treatment. Means followed by the same letters are notsignificantly different at 5% of probability according to Fisher multiplerange test.
Fig. 3. Polypeptide composition of isolated thylakoid membrane.
A sample of 1mg was loaded for SDS-PAGE. Arrow 1,2, and 3
stand for 24 KDa, 22.4KDa and 20.3KDa, respectively.
平成15年度助成研究報告集Ⅰ(平成17年3月発行)
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A1
32
45 67 8 9
1011
12 13 14 151617 18 19
20 2122 2324 25
26 27
2829 3031 32 33 34
353637 403938 41
4243
4445
46
4748
4950
51 5253
5455
56
57 58 59
60
6162
6364
B1 2 3 4
5 6 7 8 9 10
11 1213
19 20
14
1516 17 18
21 222324
2526
272829
3031 32
33
34
3536 37
3839
404142
43
45 46
47 48
44
49
50 51
5253
54
55
56 57
59
5860
IEF
pI
3.0 104.0 5.0 6.0 7.0 8.0 9.0
14.4
21.5
31.0
45.0
66.2
97.4
14.4
21.5
31.0
45.0
66.2
97.4
3.0 10
Fig. 4. Sypro ruby-stained 2-DE maps of thylakoid proteinsof O. latifolia (A) and O. rufipogon.
31
11
25
42
34
404752
5361
10
2
15262829
32
20.6
35.0
24.6
19.6
23.2
18.312.310.9
10.98.9
38.0
60.4
32.325.621.820.6
21.8
5.3
5.9
4.9
9.4
8.5
6.19.54.4
5.47.4
5.1
4.2
6.84.23.94.3
5.9
Chlorophyll A-B binding protein 6A,Chloroplast precursor(LHCⅠtypeⅠCAB-6A),Oxygen-evolving enhancer protein 2,Thylakoid lumenal 21.5 kDa protein,PhotosytemⅠassembly protein ycf3
ATP synthase gamma chain,chloroplast precursor(EC3.6.3.14)
Oxygen-evolving enhancer protein 1‐1,Chloroplast precursor(OEE1),Chlorophyll a-bbinding protein
PSⅠreaction center subunitⅡ,Chloroplast precursor(PSⅠ20 kDa subunit)
Apocytochrome f precursor, Cytochrome c biogenesis protein
Oxygen-evolving enhancer protein 2,Chloroplast precursor(OEE2),(23 kDa subunit of oxygenevolving system of PSⅡ)(23 kDa thylakoid membrane protein)(OEC23)
O. rufipogon
O. latifolia
Table 1. Characteristic of specific thylakoid membrane protein obtainedfrom 2-DE in two wild Oryza species.
Identity given in ExPASy by TagIdent tool (http://tw.expasy.org/tools/tagident.html).Search was conducted range of pI±0.1 and molecular weight±10%.
平成15年度助成研究報告集Ⅰ(平成17年3月発行)
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Study on mechanisms of salt tolerance in wild Oryza species,
O. latifolia Desv.
Seiich Mrayamaa and Sakae Agarieb a Faculty of Agriculture, University of the Ryukyus.
b Faculty of Agriculture, Saga University.
Summary
We had isolated the wild Oryza species, O. latifolia Desv., which could survive under the
conditions that the salt-tolerant cultivated rice SR26B died. The CO2 assimilation rate was
maintained under the high salinity condition that the leaf water potential was decreased with
increased NaCl level in the water-culture solution. To elucidate the mechanisms of salt tolerance in
O. latifolia, we compared the photosynthetic activities of leaves and thylakoid membranes in this
wild Oryza species with those in a salt susceptible wild Oryza species, O. rufipogon under high salt
conditions. Photosynthetic O2 evolution rate (OER) of leaves measured with liquid-phase type
oxygen electrode was maintained in O. latifolia under the salt stress condition. In O.rufipogon the
OER declined by 75% and 30% of that in non-stress leaves under 300mM and 655mMNaCl,
respectively. Whereas in O. latifolia the OER was unchanged under 300mMNaCl, and decreased
under 655mM NaCl by 60% of that in non-stress leaves. Thylakoid membrane of O. latifolia also
showed salt tolerance. The OER from isolated thylakoid membrane in O. latifolia decreased only
13% under 655mMNaCl. On the other hand, in O.rufipogon, it decreased 30% under 655mMNaCl.
The peptide compositions of thylakoid membranes examined by SDS‐PAGE showed that O.
latifolia has species-pecific proteins with 20.3 kDa and 22.4 kDa of molecular weight.
Two-dimensional electrophoresis (2-DE) of thylakoid membrane proteins showed that the 20.3 kDa
and 22.4 kDa proteins contained at least two or three proteins with different isoelectric points.
Some of them were novel proteins that had not been published in the data base.
These results suggest that thylakoid membrane of O. latifolia has high salt tolerance and this
plant can maintain photosynthetic activity under high NaCl condition. The results of SDS-PAGE
and 2-DE showed that the thylakoid membrane of O. latifolia had specific proteins which may be