Abstract
Some structural features of the yeast Gcr1 protein (Gcr1p) are analysed. The protein has three hydrophobic domains separated by hydrophilic residues (referred to as N, L, C), which correspond well with three regions of different functions. The N domain (aal-aa350) corresponds to the region (aa1-aa391) which is important for Gcr1p-Gcr1p and Gcr1p-Gcr2p interactions, while the C domain (aa570-aa785) corresponds to the region (aa631-aa785) which is important for DNA-binding. The function of the L domain (aa360-aa550) remains unknown but it contains many Ser(Thr)-Pro sequences which are potential phosphorylation sites and thus might be used for regulation of the protein function. The sequence, aa631-aa685, resembles those of multi-helical DNA-binding domains found in some transcription factors. In comparison with the DNA-binding mode of known multi-helical DNA-binding domains, DNA base-amino acid side-chain contacts at the Gcr1 site are discussed.
