Plant polyamines in reproductive activity and response to abiotic stress

被引:163
作者
Galston, AW [1 ]
KaurSawhney, R [1 ]
Altabella, T [1 ]
Tiburcio, AF [1 ]
机构
[1] UNIV BARCELONA, FAC FARM, LAB FISIOL VEGETAL, E-08028 BARCELONA, SPAIN
来源
BOTANICA ACTA | 1997年 / 110卷 / 03期
关键词
abiotic stress; arginine decarboxylase; flowering; polyamines; putrescine; reproductive activity; spermidine; spermine;
D O I
10.1111/j.1438-8677.1997.tb00629.x
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
In this review we will focus on two areas in which the accumulated evidence for a critical physiological role of polyamines is becoming compelling, i.e. reproductive activity and response to abiotic stress. Regarding reproductive behavior, it seems clear that polyamines are members of the array of internal compounds required for flower initiation, normal floral organ morphogenesis, fruit growth and fruit ripening in particular plant species. Abiotic stresses such as osmotic stress can ''turn on'' arginine decarboxylase (ADC) genes, resulting in a rapid increase in their mRNA levels. Localization of ADC enzyme in the chloroplast suggests a role of PAs in the maintenance of photosynthetic activity during senescence responses induced by osmotic stress. We envisage that the use of transgenic plants and improved molecular probes will resolve in the near future the physiological significance of stress-induced changes in PA metabolism as well as the role of these compounds in reproductive activity.
引用
收藏
页码:197 / 207
页数:11
相关论文
共 114 条
[1]  
Altabella T, 1995, PHYSIOL PLANTARUM, V95, P479, DOI 10.1111/j.1399-3054.1995.tb00866.x
[2]  
[Anonymous], 1991, BIOCH PHYSL POLYAMIN
[3]   CHARACTERIZATION OF THE S-ADENOSYLMETHIONINE DECARBOXYLASE (SAMDC) GENE OF POTATO [J].
ARIF, SAM ;
TAYLOR, MA ;
GEORGE, LA ;
BUTLER, AR ;
BURCH, LR ;
DAVIES, HV ;
STARK, MJR ;
KUMAR, A .
PLANT MOLECULAR BIOLOGY, 1994, 26 (01) :327-338
[4]  
BASTOLA DR, 1995, PLANT PHYSIOL, V109, P63, DOI 10.1104/pp.109.1.63
[5]  
BEIER H, 1987, Z NATURFORSCH C, V42, P1307
[6]   ANALYSIS OF A CDNA-ENCODING ARGININE DECARBOXYLASE FROM OAT REVEALS SIMILARITY TO THE ESCHERICHIA-COLI ARGININE DECARBOXYLASE AND EVIDENCE OF PROTEIN PROCESSING [J].
BELL, E ;
MALMBERG, RL .
MOLECULAR & GENERAL GENETICS, 1990, 224 (03) :431-436
[7]  
BERNIER G, 1993, PLANT CELL, V5, P1147, DOI 10.1105/tpc.5.10.1147
[8]  
BESFORD RT, 1993, PLANTA, V189, P201, DOI 10.1007/BF00195077
[9]   ARGININE DECARBOXYLASE IS LOCALIZED IN CHLOROPLASTS [J].
BORRELL, A ;
CULIANEZMACIA, FA ;
ALTABELLA, T ;
BESFORD, RT ;
FLORES, D ;
TIBURCIO, AF .
PLANT PHYSIOLOGY, 1995, 109 (03) :771-776
[10]  
Borrell A, 1996, PHYSIOL PLANTARUM, V98, P105, DOI 10.1111/j.1399-3054.1996.tb00680.x