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Role of NAD binding and catalytic residues in the C‐terminal binding protein corepressor
Author(s) -
Mani-Telang Priya,
Sutrias-Grau Montserrat,
Williams Geoffrey,
Arnosti David N.
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.10.011
Subject(s) - corepressor , nad+ kinase , repressor , mutant , biochemistry , binding site , chemistry , biology , enzyme , transcription factor , gene
CtBP corepressor proteins potentiate the activity of many metazoan transcriptional repressors. These proteins are homologous to prokaryotic D‐2‐hydroxyacid dehydrogenases, possessing an NAD/NADH binding fold and conserved active site residues. When expressed in Drosophila, a catalytic site mutant retains biological activity, however, we find that an NAD binding mutant lacks biological activity. The NAD mutant, similar to a dimerization mutant, is expressed at low levels, indicating that binding of NAD/NADH may affect CtBP stability. These data support the idea that the ancestral dehydrogenase activity is not required for CtBP function, and NAD binding may play a regulatory, rather than catalytic, role.