Crystal structure of the N-terminal domain of the yeast general corepressor Tup1p and its functional implications.

ABSTRACT: The yeast Cyc8p-Tup1p protein complex is a general transcriptional corepressor of genes involved in many different physiological processes. Herein, we present the crystal structure of the Tup1p N-terminal domain (residues 1-92), essential for Tup1p self-assembly and interaction with Cyc8p. This domain tetramerizes to form a novel antiparallel four-helix bundle. Coiled coil interactions near the helical ends hold each dimer together, whereas interdimeric association involves only two sets of two residues located toward the chain centers. A mutagenesis study confirmed that the nonpolar residues responsible for the association of the protomers as dimers are also required for transcriptional repression. An additional structural study demonstrated that the domain containing an Leu(62) → Arg mut

SUBMITTER: Matsumura H 

PROVIDER: S-EPMC3410994 | biostudies-literature | 2012 Aug

REPOSITORIES: biostudies-literature