Expression profiling of the Dolichos lablab lectin during germination and development of the seed

被引:3
作者
Vishweshwaraiah, Yashavanth L. [1 ]
Prakash, Balaji [1 ]
Gowda, Lalitha R. [2 ]
机构
[1] Cent Food Technol Res Inst, Dept Mol Nutr, CSIR, Mysore 570020, Karnataka, India
[2] Cent Food Technol Res Inst, CSIR, Mysore 570020, Karnataka, India
关键词
Defense proteins; Phytohormone; Storage protein; Transcript; Germination; GALACTOSE SPECIFIC LECTIN; LEGUME LECTIN; PROTEINS; BINDING; SITES;
D O I
10.1016/j.plaphy.2017.12.040
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
The temporal expression of the field bean (Dolichos lablab) galactose specific lectin, DLL-II, during germination, post-germination and seed development was evaluated using Native-PAGE followed by activity staining, immunodetection and quantitative Real Time PCR (qPCR). A rapid and steep decline in the polyphenol oxidase (PPO) and hemagglutinating activity during the initial stages of germination, which did not correlate with the slow decline in total protein was observed. During post germination period, PPO and hemagglutination activities were negligible, whereas a rapid resorption of the protein was evident. These results suggest that DLL-II is not a storage protein. The presence of mRNA in the quiescent seed and initial stages of germination are indicative of a very stable mRNA. DLL-II was expressed in high copies during seed development and increased dramatically between 10 and 20 days after flowering (DAF), suggesting a switch over stage in DLL-II expression. Transcript levels reached a maximum at the mature stage of seed development. Among the non-seed tissues examined, root showed the highest level. The high affinity binding to kinetin and indole acetic acid, the key hormones that regulate root development and its vascular differentiation add a new dimension to the physiological role of DLL-II in the seed. This finding, coupled with the PPO and hemagglutinating activity makes DLL-II, truly a multifunctional protein.
引用
收藏
页码:10 / 19
页数:10
相关论文
共 35 条
[1]   Lectin receptor kinases in plants [J].
Barre, A ;
Hervé, C ;
Lescure, B ;
Rougé, P .
CRITICAL REVIEWS IN PLANT SCIENCES, 2002, 21 (04) :379-399
[2]  
BEWLEY JD, 1990, PROG NUCLEIC ACID RE, V38, P165
[3]  
Cavada B. S., 1993, Revista Brasileira de Fisiologia Vegetal, V5, P193
[4]  
Cavada B.S., 1990, ACTA BOT BRAS, V4, P13
[5]  
CHRISPEELS MJ, 1984, PLANT PHYSIOL, V76, P791, DOI 10.1104/pp.76.3.791
[6]   CHANGES IN APPLE POLYPHENOLOXIDASE AND POLYPHENOL CONCENTRATIONS IN RELATION TO DEGREE OF BROWNING [J].
COSETENG, MY ;
LEE, CY .
JOURNAL OF FOOD SCIENCE, 1987, 52 (04) :985-989
[7]  
Webb Benjamin, 2016, Curr Protoc Bioinformatics, V54, DOI [10.1002/0471140864.ps0209s50, 10.1002/cpps.20, 10.1002/0471250953.bi0506s15, 10.1002/0471250953.bi0506s47, 10.1002/cpbi.3]
[8]  
GOWDA LR, 1994, J BIOL CHEM, V269, P18789
[9]   Carbohydrate binding, quaternary structure and a novel hydrophobic binding site in two legume lectin oligomers from Dolichos biflorus [J].
Hamelryck, TW ;
Loris, R ;
Bouckaert, J ;
Dao-Thi, MH ;
Strecker, G ;
Imberty, A ;
Fernandez, E ;
Wyns, L ;
Etzler, ME .
JOURNAL OF MOLECULAR BIOLOGY, 1999, 286 (04) :1161-1177
[10]  
Hamid Rabia., 2013, J. Appl. Pharm. Sci, V3, P93, DOI DOI 10.7324/JAPS.2013.34.S18