scholarly journals Amino acid sequence of the 26 kDa subunit of legumin-type seed storage protein of common buckwheat (Fagopyrum esculentum Moench): molecular characterization and phylogenetic analysis

2003 ◽  
Vol 63 (1) ◽  
pp. 1-5 ◽  
Author(s):  
Sangeeta Bharali ◽  
Nikhil K. Chrungoo
2004 ◽  
Vol 56 (1-2) ◽  
pp. 1-7 ◽  
Author(s):  
Mira Milisavljevic ◽  
Miroslav Konstantinovic ◽  
Jelena Brkljacic ◽  
Vesna Maksimovic

Using the modified 5?-RACE approach, a fragment containing the 955 bp long 5?- regulatory region of the buckwheat storage globulin gene (FeLEG1) has been amplified from the genomic DNA of buckwheat. The entire fragment was sequenced and the sequence analyzed by computer prediction of cis-regulatory elements possibly involved in tissue specific and developmentally controlled seed storage protein gene expression. The promoter obtained might be interesting not only for fundamental research, but also as a useful tool for biotechnological application.


2010 ◽  
Vol 62 (1) ◽  
pp. 143-151 ◽  
Author(s):  
Gordana Timotijevic ◽  
Mira Milisavljevic ◽  
Svetlana Radovic ◽  
M.M. Konstantinovic ◽  
Vesna Maksimovic

Aspartic proteinase gene (FeAP12) has been isolated from the cDNA library of developing buckwheat seeds. Analysis of its deduced amino acid sequence showed that it resembled the structure and shared high homology with typical plant aspartic proteinases (AP) characterized by the presence of a plant-specific insert (PSI), unique among APs. It was shown that FeAP12 mRNA was not present in the leaves, roots, steam and flowers, but was seed-specifically expressed. Moreover, the highest levels of FeAP12 expression were observed in the early stages of seed development, therefore suggesting its potential role in nucellar degradation.


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