N-nitrosation and denitrosation on lysine residues of histones.
نویسندگان
چکیده
Increased immunoactivity of (-nitrosolysine was detected in Western blot in peroxynitrite-reacted histones H2A, H3 and H4. The N-nitrosation may be reversible as indicated by the decreased immunoactivity via either subsequent incubation with reduced glutathione or 48-hour dialysis and 48-hour storage at 4 degrees C. Nonetheless, the biological significance of N-nitrosation of protein lysine is yet to be proven.
منابع مشابه
Redox-Sensitivity and Site-Specificity of S- and N- Denitrosation in Proteins
BACKGROUND S-nitrosation--the formation of S-nitrosothiols (RSNOs) at cysteine residues in proteins--is a posttranslational modification involved in signal transduction and nitric oxide (NO) transport. Recent studies would also suggest the formation of N-nitrosamines (RNNOs) in proteins in vivo, although their biological significance remains obscure. In this study, we characterized a redox-base...
متن کاملN-nitrosations of basic amino acid residues in polypeptide.
Changes in the electrophoretic pattern were noted in the products of polypeptides of identical basic amino acids preincubated with reactive or degraded PN, suggesting the occurrence of N-nitrosation of the epsilon-amino group of lysine, the guanido group of arginine and the imidazole group of histidine. Additionally, increase in the N-nitroso immunoreactivity of preincubated histones H2A and H2...
متن کاملNε-Formylation of lysine is a widespread post-translational modification of nuclear proteins occurring at residues involved in regulation of chromatin function
Post-translational modification of histones and other chromosomal proteins regulates chromatin conformation and gene activity. Methylation and acetylation of lysyl residues are among the most frequently described modifications in these proteins. Whereas these modifications have been studied in detail, very little is known about a recently discovered chemical modification, the N(epsilon)-lysine ...
متن کاملAmino acid sequence and sequence variability of the amino-terminal regions of lysine-rich histones.
The amino acid sequence has been determined for the first 72 residues of a lysine-rich histone from rabbit thymus. These are the residues contained in a fragment released from the histone by treatment with N-bromosuccinimide. Peptides derived by tryptic, thermolysin, and chymotryptic digestion of this 72-residue fragment were used to reconstruct the total sequence. Analysis of the sequence reve...
متن کاملMethylation of nuclear proteins by dimethylnitrosamine and by methionine in the rat in vivo.
1. The incorporation of methyl groups into histones from dimethylnitrosamine and from methionine was studied by injection of the labelled compounds, isolation of rat liver and kidney histones, and analysis of hydrolysates by column chromatography. 2. Labelled methionine gave rise to labelled in-N-methyl-lysine, di-in-N-methyl-lysine and an amino acid presumed to be omega-N-methyl-arginine. 3. A...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
عنوان ژورنال:
- Frontiers in bioscience : a journal and virtual library
دوره 9 شماره
صفحات -
تاریخ انتشار 2004