Proteomic analysis of early responsive resistance proteins of wheat (Triticum aestivum) to yellow rust (Puccinia striiformis f. sp tritici) using ProteomeLab PF2D

WOS: 000317715600004Wheat (Triticum aestivum L.) yellow rust, caused by Puccinia striiformis f. sp. tritici (Pst), is one of the most destructive diseases of wheat worldwide. To clarify the molecular details and components of the resistance response in wheat offers further possibilities to combat yellow rust. In this study, differentially regulated early response proteins in wheat leaves infected by Pst isolates were investigated by proteomic approaches. Total proteins extracts from leaves harvested at 24 hour post inoculation (hpi) were separated by two dimensional liquid chromatography system, ProteomeLab PF2D. Following PF2D analysis, six hundred and thirty-seven protein peaks were compared one by one between protein patterns obtained from pathogen-and mock-inoculated leaf tissue. Among those differentially expressed 33 proteins were identified in Pst-infected plants as compared with mock-inoculated controls by nanoLC-ESI-MS/MS. Six proteins were exhibited homology to fungal proteins. Two fungal proteins, including E3 ubiquitin protein ligase and Ubiquitin-like protein, are important members of ubiquitin-proteasome system which the importance of the its proteolytic function in regulating the virulence of pathogenic fungi has just been realized recently. Other identified 27 proteins were host proteins in response to Pst and classified in five groups based on their roles in diverse biological processes. The results indicated that identified defence related proteins such as pathogene related protein 1 and 4 (PR1, PR4), Glutathione S transferase (GST) are major component for systemic acquired resistance (SAR) which is one of the strong disease resistance form in plants and appears within several days following the initial pathogen attack.TUBITAK, COST programmeTurkiye Bilimsel ve Teknolojik Arastirma Kurumu (TUBITAK) [109T293]This study was supported by TUBITAK, COST programme 109T293 project. We thank Kadir Akan, Ayse Yildiz and Lutfi Cetin for their help during plant inoculation and sampling. We also thank Abdulmecit Gokce and Yavuz Ozturk for their technical support for PF2D as well as Konca Bulut and Rahmi Buyukkeskin for their experimental assistance

Proteomic investigation of compatible interaction between wheat and yellow rust

WOS: 000209805600356

Proteomic investigation of compatible interaction between wheat and yellow rust

WOS: 000209805600532

Proteome profiling of the compatible interaction between wheat and stripe rust

WOS: 000379860300018Over the last decade, comparative molecular profiling studies between compatible and incompatible plant-pathogen interactions have shown that susceptible response of the host to a pathogen requires factors that promote disease development. In this study, we examined proteome profiles during a compatible interaction between wheat and stripe rust. A 2D-LC system (ProteomeLab PF2D) was used for protein separation and to compare the proteome from infected and control samples. More than 700 protein peaks at each time point were compared between pathogen- and mock-inoculated samples. Selected proteins, with significant differences in abundance were identified by nanoLC-ESI- MS/MS and generated spectra were searched against the wheat protein databases from UniProt, and NCBI and the Puccinia database from The Broad Institute. In total, the identified proteins comprised of 62 % wheat and 38 % Pst proteins. All identified proteins were searched by bioinformatics-based algorithms to detect their subcellular localization and signal peptide motifs which have the potential to catch the candidate effector proteins. The wheat proteins were classified based on their function. Although a compatible interaction, many wheat proteins, such as antioxidants, PRs and cold-responsive proteins, are implicated in defense and stress tolerance. On the pathogen side, 64 proteins were identified, and included some important pathogenicity proteins that can play role in pathogen virulence and suppress the host defense. In addition, we discovered that nine proteins have a signal sequence and three of the hypothetical fungal proteins, PGTG_11681T0, PGTG_07231T0 and CBH50687.1, have been tentatively identified as candidate effectors.TUBITAKTurkiye Bilimsel ve Teknolojik Arastirma Kurumu (TUBITAK) [109 T293]This study was supported by TUBITAK, COST programme 109 T293 project. We thank Kadir Akan, Aysc Yildiz and Lutfi Cetin for their help during plant inoculation and sampling. We also thank Abdulmecit Gokce and Yavuz Ozturk for their technical support for PF2D as well as Konca Bulut and Rahmi Buyukkeskin for their experimental assistance