| Abstract Detail
Emerging Technologies Ramu Subramanian, Saravanan [1], Bhattacharyya, Madan Kumar [2]. Comparative phosphoproteomics of the soybean-Phytophthora sojae interaction: Immobilized metal affinity chromatography in identifying candidate phosphoproteins. Phosphorylation plays a regulatory role in activating many proteins for various biological functions. Many of these proteins could be less abundant; and therefore, their isolation is arduous. We have utilized the zirconium ion (Zr4+) based immobilized metal affinity chromatography (IMAC) in isolating candidate soybean proteins that are differentially phosphorylated following infection with the oomycete pathogen, Phytophthora sojae. In order to reduce the artifacts arisen from binding of acidic proteins during enrichment, protein samples were esterified prior to IMAC. The esterification step prior to IMAC did not alter the overall phosphoproteomes of the infected and control tissues. This step however enhanced the efficacy of IMAC presumably by eliminating undesirable binding of metal ions to acidic residues. Twelve proteins, presumably differentially phosphorylated in infected and healthy tissues, were identified by conducting 2D-PAGE and ESI-MS/MS analyses. The identified proteins were mostly metabolism and defense related. By conducting mass spectrometric characterization and immunoprecipitation experiments we have shown that Cu-Zn superoxide dismutase (SOD), identified in this investigation, is phosphorylated in P. sojae-infected tissues.
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1 - Iowa State University, Department of Agronomy, G 302 Agron Hall, Ames, Iowa, 50014, USA
2 - Iowa State University, Department of Agronomy
Keywords:
phosphoproteomics
plant pathogen interaction.
Presentation Type: Plant Biology Abstract
Session: P
Location: Exhibit Hall (Northeast, Southwest & Southeast)/Hilton
Date: Sunday, July 8th, 2007
Time: 8:00 AM
Number: P44021
Abstract ID:2544 |
