Identification of SUMOylated proteins in neuroblastoma cells after treatment with hydrogen peroxide or ascorbate
The small ubiquitin-like modifier (SUMO) proteins have been implicated in the pathology of a number of diseases, including neurodegenerative diseases. The conjugation machinery for SUMOylation consists of a number of proteins which are redox sensitive. Here, under oxidative stress (100 μM hydrogen p...
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Published in | BMB reports Vol. 43; no. 11; pp. 720 - 725 |
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Main Author | |
Format | Journal Article |
Language | Korean |
Published |
생화학분자생물학회
30.11.2010
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Subjects | |
Online Access | Get full text |
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Summary: | The small ubiquitin-like modifier (SUMO) proteins have been implicated in the pathology of a number of diseases, including neurodegenerative diseases. The conjugation machinery for SUMOylation consists of a number of proteins which are redox sensitive. Here, under oxidative stress (100 μM hydrogen peroxide), antioxidant (100 μM ascorbate) or control conditions 169 proteins were identified by electospray ionisation fourier transform ion cyclotron resonance mass spectrometry. The majority of these proteins (70%) were found to contain SUMOylation consensus sequences. From the remaining proteins a small number (12%) were found to contain possible SUMO interacting motifs. The proteins identified included DNA and RNA binding proteins, structural proteins and proteasomal proteins. Several of the proteins identified under oxidative stress conditions had previously been identified as SUMOylated proteins, thus validating the method presented. [BMB reports 2010; 43(11): 720-725] |
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Bibliography: | Korean Society for Biochemistry and Molecular Biology KISTI1.1003/JNL.JAKO201001039069147 |
ISSN: | 1976-6696 1976-670X |