Redox modifications of the C-terminal cysteine residue cause structural changes in S100A1 and S100B proteins.
S100 is a family of small, acidic, calcium binding proteins involved in the control of a multitude of intra- and extracellular processes, including many pathologies. The application of the analytical methodology based on the combination of RP HPLC and ESI-MS allowed for the characterization of S-nitrosylation and S-glutathionylation in two representative S100 proteins: S100A1 and S100B. The GSNO related S-nitrosylation of the conserved C-terminal cysteine is strongly activated by the binding of Ca(II) to S100A1 and of Ca(II) and Zn(II) to S100B. This modification results in a global alteration of protein structure, as demonstrated by a variety of techniques. The presented results provide a mechanistic basis for further studies of the function of S100 proteins in the control of redox-based and metal-based signal transduction.
Zhukova
Liliya
L
Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawinskiego 5a, 02-106, Warszawa, Poland.
Zhukov
Igor
I
Bal
Wojciech
W
Wyslouch-Cieszynska
Aleksandra
A
D000818:Animals; D002851:Chromatography, High Pressure Liquid; D003545:Cysteine / Q000737:chemistry*; D006801:Humans; D009363:Neoplasm Proteins / Q000737:chemistry*; D009414:Nerve Growth Factors / Q000737:chemistry*; D010084:Oxidation-Reduction; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D064568:S100 Calcium Binding Protein beta Subunit; D009418:S100 Proteins / Q000737:chemistry*; D021241:Spectrometry, Mass, Electrospray Ionization
D009363:Neoplasm Proteins; D009414:Nerve Growth Factors; D011506:Proteins; D064568:S100 Calcium Binding Protein beta Subunit; D009418:S100 Proteins; C579160:S100B protein, human; C056201:urine S 100 protein, alpha subunit, human; D003545:Cysteine