Mass spectrometry approaches for the redox characterization of protein cysteine residues the case of the transcription factor Pax-8.
Regulation of protein structure and function by redox reactions has emerged as an exciting area of research study. The transduction of a redox signal into a biological response can be mediated in several ways, but a principal mechanism involves the modification of protein cysteine (Cys) residues. Several transcription factors, such as NF-kappaB, Egr-1, AP-1, and Pax, are regulated through redox-based mechanisms. Thus, redox regulation represents a key issue in specifically controlling gene expression. This study describes the combined use of MS procedures and protein-functional assays to investigate the redox state of a protein-regulating gene expression in thyroid, namely Pax-8, a member of the Pax family of transcription factors. Molecular characterization of the modified cysteine residues after various oxidative insults provided information on the mechanisms controlling protein-functional properties.
Proteomics and Mass Spectrometry Laboratory, ISPAAM, National Research Council, Naples, Italy.
Andrea
A
Scaloni
Gianluca
G
Tell
D003545:Cysteine / Q000032:analysis* / Q000378:metabolism; D006367:HeLa Cells; D006801:Humans; D013058:Mass Spectrometry / Q000379:methods*; D008954:Models, Biological; D010084:Oxidation-Reduction; D000072636:PAX8 Transcription Factor; D051761:Paired Box Transcription Factors / Q000737:chemistry* / Q000378:metabolism*; D010449:Peptide Mapping / Q000379:methods; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D013329:Structure-Activity Relationship; D014157:Transcription Factors / Q000737:chemistry / Q000378:metabolism
D000072636:PAX8 Transcription Factor; C083325:PAX8 protein, human; D051761:Paired Box Transcription Factors; D011506:Proteins; D014157:Transcription Factors; D003545:Cysteine