Mr. Satya Prakash Chaurasia , Master - University of Delhi - Junior Research Fellow

Mr. Satya Prakash Chaurasia

Master

University of Delhi

Junior Research Fellow

Delhi, Delhi | India

Main Specialties: Biology

Additional Specialties: Molecular Biology

Mr. Satya Prakash Chaurasia , Master - University of Delhi - Junior Research Fellow

Mr. Satya Prakash Chaurasia

Master

Introduction

Primary Affiliation: University of Delhi - Delhi, Delhi , India

Specialties:

Additional Specialties:


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Number of Publications

3

Publications

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444

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Number of Article Reads

11

Reads

Education

Phd Research Scholar

Publications

3Publications

11Reads

Identification of Major Redox Modulated Proteins from Brassica juncea Seedlings, and demonstration of differential sensitivity of RuBisCO large and small subunit towards oxidative stress [abstract]

JPP. 2017 Nov 4(8); 71

Journal of Proteins and Proteomics

The activity of proteins is also regulated by PTMs (post translational modifications) including the thiol–disulphide exchange, a redox modulation. Studies to analyze reactive oxygen species (ROS), particularly, hydrogen peroxide (H2O2) induced changes in the gene expression are reported in good number, but attempts to detect H2O2 modified proteins are comparatively very few. Here, an effort was made to identify proteins undergoing thiol–disulphide exchange in Brassica juncea seedlings crude protein extract using 2D Redox SDS PAGE technique after H2O2 (10 mM) treatment for 30 min. In all, 17 spots showed redox response of which 11 were subjected to MS analysis resulting in the identification 13 proteins. These thirteen redox responsive proteins included 6 Cruciferin subunits, 3 RuBisCO (Ribulose-1,5-bisphosphate carboxylase/oxygenase) large subunits, one NLI [Nuclear LIM (Lin11, Isl-1 & Mec-3 domains)] interacting protein phosphatase and Myrosinase. Redox modification of RuBisCO large subunit was further confirmed by western blotting. The small subunit of RuBisCO was not redox responsive to H2O2. All the targets of H2O2 except NLI interacting protein (which contains two cysteines) showed oxidation sensitive cysteines by in silico analysis. Interactome analysis was done using STRING (Search Tool for the Retrievel of Interacting Genes/Proteins) database. Interestingly, the interactome of myrosinase and cruciferin indicated that they may have additional role(s) beside their well-known functions in the abiotic stress response and seedling development respectively. Cruciferin showed interactions with stress associated proteins like 2-cys peroxiredoxin & defensing-like protein 192. Similarly, myrosinase showed interactions with nitrilase and cytochrome p450 indicating involvement in nitrogen metabolism and/or hormone biosynthesis. This simple approach can be used to detect and validate major stress mediated redox changes in other plants.

View Article
November 2017
1 Read

Identification and In Silico Analysis of Major Redox Modulated Proteins from Brassica juncea Seedlings Using 2D Redox SDS PAGE (2-Dimensional Diagonal Redox Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis)

Chaurasia, S.P. & Deswal, R. Protein J (2017). doi:10.1007/s10930-017-9698-x

The Protein Journal

The thiol–disulphide exchange regulates the activity of proteins by redox modulation. Many studies to analyze reactive oxygen species (ROS), particularly, hydrogen peroxide (H2O2) induced changes in the gene expression have been reported, but efforts to detect H2O2 modified proteins are comparatively few. Two-dimensional diagonal redox sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS PAGE) was used to detect polypeptides which undergo thiol–disulphide exchange in Brassica juncea seedlings following H2O2 (10 mM) treatment for 30 min. Eleven redox responsive polypeptides were identified which included cruciferin, NLI [Nuclear LIM (Lin11, Isl-1 & Mec-3 domains)] interacting protein phosphatase, RuBisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase) large subunit, and myrosinase. Redox modulation of RuBisCO large subunit was further confirmed by western blotting. However, the small subunit of RuBisCO was not affected by these redox changes. All redox modulated targets except NLI interacting protein (although it contains two cysteines) showed oxidation sensitive cysteines by in silico analysis. Interestingly, interactome of cruciferin and myrosinase indicated that they may have additional function(s) beside their well-known roles in the seedling development and abiotic stress respectively. Cruciferin showed interactions with stress associated proteins like defensing-like protein 192 and 2-cys peroxiredoxin. Similarly, myrosinase showed interactions with nitrilase and cytochrome p450 which are involved in nitrogen metabolism and/or hormone biosynthesis. This simple procedure can be used to detect major stress mediated redox changes in other plants.

View Article
February 2017
68 Reads

Following

Sougrakpam Yaiphabi Chanu
Sougrakpam Yaiphabi Chanu

University of Delhi