Oxidation of glyceraldehyde-3-phosphate dehydrogenase enhances its binding to nucleic acids

Enzymes of the central carbon metabolism: Are they linkers between transcription, DNA replication, and carcinogenesis?

“…GAPDH was identified as a specific mRNAbinding protein important for regulation of gene translation [74]. Moreover, the enhancement of GAPDH binding with total transfer RNA or with total DNA was observed after oxidation of SH-groups of the active site of this enzyme [75]. Oxidatively modified GAPDH was found to be involved in regulation of RNA splicing, most probably through interaction with the specific catalytic complex [76].…”

Reactive oxygen species damaged human serum albumin in patients with type 1 diabetes mellitus: Biochemical and immunological studies

“…A number of studies indicate a strong role for increases in protein oxidation as a primary cause of cellular dysfunction observed during aging and age related neurodegenerative diseases (Tabner et al, 2001) such as Alzheimer's disease, Parkinson's disease, and some other possible protein conformational diseases. Inhibition of a wide array of enzyme activities has been reported (Arutyunova et al, 2003). Modification of structural protein can also lead to loss of function.…”

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) interacts with apurinic/apyrimidinic sites in DNA

“…NAD + inhibits binding of GAPDH with DNA [16] and RNA [17]; this may indicate participation of the NAD + -binding site in these interactions. Oxidation of SHgroups in the active site of GAPDH increases its binding with DNA and tRNA [18]. In addition, oxidation of GAPDH decreases its affinity to NAD + , but not to NADH, which inhibits binding of oxidized GAPDH with DNA more effectively than NAD + [18].…”