Restriction of chlorophyll synthesis due to expression of glutamate 1 semialdehyde aminotransferase antisense RNA does not reduce the light-harvesting antenna size in tobacco

被引:27
作者
Hartel, H [1 ]
Kruse, E [1 ]
Grimm, B [1 ]
机构
[1] INST PFLANZENGENET & KULTURPFLANZENFORSCH,D-06466 GATERSLEBEN,GERMANY
关键词
D O I
10.1104/pp.113.4.1113
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
The formation of 5-aminolevulinate is a key regulatory step in tetrapyrrole biosynthesis. In higher plants, glutamate 1-semialdehyde aminotransferase (GSA-AT) catalyzes the last step in the sequential conversion of glutamate to 5-aminolevulinate. Antisense RNA synthesis for GSA-AT leads to reduced GSA-AT protein levels in tobacco (Nicotiana tabacum L.) plants. We have used these transgenic plants for studying the significance of chlorophyll (Chl) availability for assembly of the light-harvesting apparatus. To avoid interfering photoinhibitory stress, plants were cultivated under a low photon flux density of 70 mu mol photons m(-2) s(-1). Decreased GSA-AT expression does not seem to suppress other enzymic steps in the Chl pathway, indicating that reduced Chl content in transgenic plants (down to 12% of the wild-type level) is a consequence of reduced GSA-AT activity. Chl deficiency correlated with a drastic reduction in the number of photosystem I and photosystem II reaction centers and their surrounding antenna on a leaf area basis. Different lines of evidence from the transgenic plants indicate that complete assembly of light-harvesting pigment-protein complexes is given preference over synthesis of new reaction center/core complexes, resulting in fully assembled photosynthetic units with no reduction in antenna size. Photosynthetic oxygen evolution rates and in vivo Chl fluorescence showed that GSA-AT antisense plants are photochemically competent. Thus, we suggest that under the growth conditions chosen during this study, plants tend to maintain their light-harvesting antenna size even under limited Chl supply.
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页码:1113 / 1124
页数:12
相关论文
共 45 条
[1]   RESOLUTION OF 16 TO 20 CHLOROPHYLL PROTEIN COMPLEXES USING A LOW IONIC-STRENGTH NATIVE GREEN GEL SYSTEM [J].
ALLEN, KD ;
STAEHELIN, LA .
ANALYTICAL BIOCHEMISTRY, 1991, 194 (01) :214-222
[2]   LIGHT-INDUCED BIOGENESIS OF LIGHT-HARVESTING COMPLEX-I (LHC-I) DURING CHLOROPLAST DEVELOPMENT IN BARLEY (HORDEUM-VULGARE) - STUDIES USING CDNA CLONES OF THE 21-KILODALTON AND 20-KILODALTON LHC-I APOPROTEINS [J].
ANANDAN, S ;
MORISHIGE, DT ;
THORNBER, JP .
PLANT PHYSIOLOGY, 1993, 101 (01) :227-236
[3]   TRANSBILAYER ORGANIZATION OF THE CHLOROPHYLL-PROTEINS OF SPINACH THYLAKOIDS [J].
ANDERSSON, B ;
ANDERSON, JM ;
RYRIE, IJ .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1982, 123 (02) :465-472
[4]   THE EFFECT OF LIGHT ON THE BIOSYNTHESIS OF THE LIGHT-HARVESTING CHLOROPHYLL A-B PROTEIN - EVIDENCE FOR THE REQUIREMENT OF CHLOROPHYLL A FOR THE STABILIZATION OF THE APOPROTEIN [J].
APEL, K ;
KLOPPSTECH, K .
PLANTA, 1980, 150 (05) :426-430
[5]   REORGANIZATION OF THE PHOTOSYSTEM-II UNIT IN DEVELOPING THYLAKOIDS OF HIGHER-PLANTS AFTER TRANSFER TO DARKNESS - CHANGES IN CHLOROPHYLL-B, LIGHT-HARVESTING CHLOROPHYLL PROTEIN-CONTENT, AND GRANA STACKING [J].
ARGYROUDIAKOYUNOGLOU, JH ;
AKOYUNOGLOU, A ;
KALOSAKAS, K ;
AKOYUNOGLOU, G .
PLANT PHYSIOLOGY, 1982, 70 (05) :1242-1248
[6]  
Beale S.I., 1990, BIOSYNTHESIS HEME CH, P287
[7]   Members of a low-copy number gene family encoding glutamyl-tRNA reductase are differentially expressed in barley [J].
Bougri, O ;
Grimm, B .
PLANT JOURNAL, 1996, 9 (06) :867-878
[8]   THE EFFECTS OF CATIONS AND TRYPSIN ON EXTRACTION OF CHLOROPHYLL PROTEIN COMPLEXES BY OCTYL GLUCOSIDE [J].
CAMM, EL ;
GREEN, BR .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1982, 214 (02) :563-572
[9]   SINGLE-STEP METHOD OF RNA ISOLATION BY ACID GUANIDINIUM THIOCYANATE PHENOL CHLOROFORM EXTRACTION [J].
CHOMCZYNSKI, P ;
SACCHI, N .
ANALYTICAL BIOCHEMISTRY, 1987, 162 (01) :156-159
[10]   ORGANIZATION OF THE LIGHT-HARVESTING COMPLEX OF PHOTOSYSTEM-I AND ITS ASSEMBLY DURING PLASTID DEVELOPMENT [J].
DREYFUSS, BW ;
THORNBER, JP .
PLANT PHYSIOLOGY, 1994, 106 (03) :841-848