Accumulation of high levels of free amino acids in soybean seeds through integration of mutations conferring seed protein deficiency

被引:103
作者
Takahashi, M
Uematsu, Y
Kashiwaba, K
Yagasaki, K
Hajika, M
Matsunaga, R
Komatsu, K
Ishimoto, M [1 ]
机构
[1] Natl Agr Res Ctr, Hiroshima 7218514, Japan
[2] Natl Agr Res Ctr, Kumamoto 8611192, Japan
[3] Ibaraki Univ, Sch Agr, Ibaraki 3000393, Japan
[4] Natl Inst Agrobiol Sci, Tsukuba, Ibaraki 3058602, Japan
[5] Nagano Chushin Agr Expt Stn, Nagano 3996461, Japan
关键词
glycine; glycinin; beta-conglycinin; storage protein; nitrogen content; mutation;
D O I
10.1007/s00425-003-1026-3
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Soybean (Glycine max [L] Merr.) seeds are rich in protein, most of which is contributed by the major storage proteins glycinin (11S globulin) and beta-conglycinin (7S globulin). Null mutations for each of the subunits of these storage proteins were integrated by crossbreeding to yield a soybean line that lacks both glycinin and beta-conglycinin components. In spite of the absence of these two major storage proteins, the mutant line grew and reproduced normally, and the nitrogen content of its dry seed was similar to that for wild-type cultivars. However, protein bodies appeared underdeveloped in the cotyledons of the integrated mutant line. Furthermore, whereas free amino acids contribute only 0.3-0.8% of the seed nitrogen content of wild-type varieties, they constituted 4.5-8.2% of the seed nitrogen content in the integrated mutant line, with arginine (Arg) being especially enriched in the mutant seeds. Seeds of the integrated mutant line thus appeared to compensate for the reduced nitrogen content in the form of glycinin and beta-conglycinin by accumulating free amino acids as well as by increasing the expression of certain other seed proteins. These results indicate that soybean seeds are able to store nitrogen mostly in the form of either proteins or free amino acids.
引用
收藏
页码:577 / 586
页数:10
相关论文
共 49 条
[1]   Genomic organization of glycinin genes in soybean [J].
Beilinson, V ;
Chen, Z ;
Shoemaker, RC ;
Fischer, RL ;
Goldberg, RB ;
Nielsen, NC .
THEORETICAL AND APPLIED GENETICS, 2002, 104 (6-7) :1132-1140
[2]   Mapping QTL for seed protein and oil content in eight soybean populations [J].
Brummer, EC ;
Graef, GL ;
Orf, J ;
Wilcox, JR ;
Shoemaker, RC .
CROP SCIENCE, 1997, 37 (02) :370-378
[3]   X-RAY CRYSTAL-STRUCTURE OF THE SOYBEAN AGGLUTININ CROSS-LINKED WITH A BIANTENNARY ANALOG OF THE BLOOD-GROUP-I CARBOHYDRATE ANTIGEN [J].
DESSEN, A ;
GUPTA, D ;
SABESAN, S ;
BREWER, CF ;
SACCHETTINI, JC .
BIOCHEMISTRY, 1995, 34 (15) :4933-4942
[4]   Arginase is inoperative in developing soybean embryos [J].
Goldraij, A ;
Polacco, JC .
PLANT PHYSIOLOGY, 1999, 119 (01) :297-303
[5]   Arginine degradation by arginase in mitochondria of soybean seedling cotyledons [J].
Goldraij, A ;
Polacco, JC .
PLANTA, 2000, 210 (04) :652-658
[6]   A 62-KD SUCROSE BINDING-PROTEIN IS EXPRESSED AND LOCALIZED IN TISSUES ACTIVELY ENGAGED IN SUCROSE TRANSPORT [J].
GRIMES, HD ;
OVERVOORDE, PJ ;
RIPP, K ;
FRANCESCHI, VR ;
HITZ, WD .
PLANT CELL, 1992, 4 (12) :1561-1574
[7]  
Hajika M, 1998, BREEDING SCI, V48, P383
[8]  
Hajika M, 1996, BREEDING SCI, V46, P385
[9]   SOYBEAN BETA-CONGLYCININ GENES ARE CLUSTERED IN SEVERAL DNA REGIONS AND ARE REGULATED BY TRANSCRIPTIONAL AND POSTTRANSCRIPTIONAL PROCESSES [J].
HARADA, JJ ;
BARKER, SJ ;
GOLDBERG, RB .
PLANT CELL, 1989, 1 (04) :415-425
[10]  
HARADA K, 1983, JPN J BREED, V33, P23