Abstract
Histones are DNA protective proteins and may adopt different structures under nitrosative stress. Peroxynitrite is a powerful oxidant and nitrating agent and has in vivo existence. In this communication, we report effect of peroxynitrite-mediated oxidation and nitration on the structure of calf thymus H3 histone. Fine details of peroxynitrite-modified H3 histone were worked out by UV, fluorescence, circular dichroism and Fourier-transformed infrared spectroscopy and polyacrylamide gel. The results revealed that peroxynitrite-mediated nitration and oxidation in H3 histone produced partially folded structure in comparison to the intrinsically disordered structure of native H3 histone. It may be concluded that the H3 histone, constituent of core histones, is highly sensitive to peroxynitrite and can adopt different structures under nitrosative stress in order to protect the packaged DNA from the deleterious insult of peroxynitrite.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
More From: International Journal of Biological Macromolecules
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.