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Protein Microarray Characterization of the <i>S</i> -Nitrosoproteome
Lee, Yun-Il,Giovinazzo, Daniel,Kang, Ho Chul,Lee, Yunjong,Jeong, Jun Seop,Doulias, Paschalis-Thomas,Xie, Zhi,Hu, Jianfei,Ghasemi, Mehdi,Ischiropoulos, Harry,Qian, Jiang,Zhu, Heng,Blackshaw, Seth,Dawso The American Society for Biochemistry and Molecula 2014 Molecular and Cellular Proteomics Vol.13 No.1
<P>Nitric oxide (NO) mediates a substantial part of its physiologic functions via <I>S</I>-nitrosylation, however the cellular substrates for NO-mediated <I>S</I>-nitrosylation are largely unknown. Here we describe the <I>S</I>-nitrosoproteome using a high-density protein microarray chip containing 16,368 unique human proteins. We identified 834 potentially <I>S</I>-nitrosylated human proteins. Using a unique and highly specific labeling and affinity capture of <I>S</I>-nitrosylated proteins, 138 cysteine residues on 131 peptides in 95 proteins were determined, defining critical sites of NO's actions. Of these cysteine residues 113 are novel sites of <I>S</I>-nitrosylation. A consensus sequence motif from these 834 proteins for <I>S</I>-nitrosylation was identified, suggesting that the residues flanking the <I>S</I>-nitrosylated cysteine are likely to be the critical determinant of whether the cysteine is <I>S</I>-nitrosylated. We identify eight ubiquitin E3 ligases, RNF10, RNF11, RNF41, RNF141, RNF181, RNF208, WWP2, and UBE3A, whose activities are modulated by <I>S</I>-nitrosylation, providing a unique regulatory mechanism of the ubiquitin proteasome system. These results define a new and extensive set of proteins that are susceptible to NO regulation via <I>S</I>-nitrosylation. Similar approaches could be used to identify other post-translational modification proteomes.</P>