Proteom ic characterization o f soybean lea f proteins from cultivar D T 2000 with rust-resistant ability in Vietnam

A

International Journal of Biọsciences I IJB I

ISSN: 2220-6655 (Print), 2222-5234 (Online)

http://www.innspub.net

Vol. 6, No. 2, p. 468-477, 2015

INNSPUB

RESEARCH PAPER

Proteomic characterization of soybean leaf proteins from

cultivar DT2000 with rust-resistant ability in Vietnam

Vu Thanh T r a 1, Tran Thi Phuong Lien®, Chu Hoang M au1’

'T hai Nguyen University, Vietnam

-Institute o f Biotechnology, Academy o f Science and Technolog)!, Vietnam

K eyw o rd s: Leaf proteins, Phakopsora pachyrhizi Syd., proteomics, soybean, rust-resistant ability.

h ttp ://d x .d o i.o r g / 10. 1ÍÌ6 9 2 /i jb /6.2.468-477 A rticle published on Ja n u a ry 2.9, 2015

Recently, proteomics has become one of the most promising and powerful tools for the proteome identification

in plant cells. In this study, a proteomics approach was used to analyze and characterize soybean leaf proteins

from a soybean rust (Phakopsora pcichyrhizi Syd.) resistant soybean cultivar DT2000. Initially, nine-day-old

leaf proteins were extracted from cultivar DT2000 and then separated by two-dimensional polyacrylamide gel

electrophoresis (2DE). The collected protein spots were cut out, treated, trypsin-digested, and analyzed by using

two-dimensional nano-liquid chromatography (LC) coupled online with tandem mass spectrometry. Results

showed that 119 protein spots were found in 2DE gels. Of these, 35 leaf proteins were characterized from the

cultivar DT2000. The identified proteins were classified into nine functional groups by Gene Ontology as

follows: photosynthesis (29%), energy (17%), glycolysis (11%), storage (9%), metabolism (8%), transport (8%),

transcription (8%), disease/defense (8%) and unknown (6%). Especially, out of 35 characterized proteins from

the cultivar DT2000, three proteins related to the defense and disease resistance were discovered. The results of

our study indicated that the 2DE combined with nanoLC and coupled with tandem mass spectrometry (ESI Q

TRAP MSMS) analyze was a promising approach for the identification of soybean proteins.

Abstract

* Corresponding Author: Chu Hoang Mau chuhoanc;[email protected]