The native GCN4 leucine-zipper domain does not uniquely specify a dimeric oligomerization state.

ABSTRACT: The dimerization domain of the yeast transcription factor GCN4, one of the first coiled-coil proteins to be structurally characterized at high resolution, has served as the basis for numerous fundamental studies on α-helical folding. Mutations in the GCN4 leucine zipper are known to change its preferred oligomerization state from dimeric to trimeric or tetrameric; however, the wild-type sequence has been assumed to encode a two-chain assembly exclusively. Here we demonstrate that the GCN4 coiled-coil domain can populate either a dimer or trimer fold, depending on environment. We report high-resolution crystal structures of the wild-type sequence in dimeric and trimeric assemblies. Biophysical measurements suggest populations of both oligomerization states under certain experimental conditi

SUBMITTER: Oshaben KM 

PROVIDER: S-EPMC3535301 | biostudies-literature | 2012 Nov

REPOSITORIES: biostudies-literature