The IGBB is a member of the NIH-funded Mississippi IDeA Network of Biomedical Research Excellence (Mississippi INBRE or MS-INBRE), a program designed to build biomedical infrastructure throughout the state. Through MS-INBRE, Mississippi students and faculty at Mississippi's undergraduate institutions are (1) trained in biomedical research techniques, (2) given the opportunity to work with top researchers at Mississippi's major research universities, (3) afforded access to state-of-the-art bioscience equipment, and (4) provided with assistance in preparing grant proposals. The IGBB serves as the MS-INBRE proteomics/computational biology core. For more information about MS-INBRE, click here.
Dr. Nisarga K. NarayanaPostdoctoral Associate
GENOMICS
email(662) 617-1858
352 Dorman Hall
Proteome and phosphoproteome differential expression under salinity stress in rice (Oryza sativa) roots
IGBB Authors:
Zhaohua PengPUBLICATION YEAR:
2007IMPACT FACTOR:
6.144CITATION COUNT:
157Chitteti BR, Peng Z (2007) Proteome and phosphoproteome differential expression under salinity stress in rice (Oryza sativa) roots.
Journal of Proteome Research 6(5): 1718-1727.
DOI:
10.1021/pr060678zEID:
2-s2.0-34249315763PMID: 17385905
DOWNLOAD PDFABSTRACTSalinity stress is a major abiotic stress that limits agriculture productivity worldwide. Rice is a model plant of monocotyledons, including cereal crops. Studies have suggested a critical role of protein phosphorylation in salt stress response in plants. However, the phosphoproteome in rice, particularly under salinity stress, has not been well studied. Here, we use Pro-Q Diamond Phosphoprotein Stain to study rice phosphoproteome differential expression under salt stress. Seventeen differentially upregulated and 11 differentially downregulated putative phosphoproteins have been identified. Further analyses indicate that 10 of the 17 upregulated proteins are probably upregulated at post-translational level instead of the protein concentration. Meanwhile, we have identified 31 salt stress differentially regulated proteins using SYPRO Ruby stain. While eight of them are known salt stress response proteins, the majority has not been reported in the literature. Our studies have provided valuable new insight into plant response to salinity stress.
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