A pivotal role of the coiled coil of Sir4.
The C terminus of Sir4 forms a coiled-coil structure. The coiled-coil domain is responsible for the dimerization of Sir4 and contains the binding site of Sir3. Structural and biochemical analyses of the Sir4 coiled-coil domain provide important insights into the molecular mechanisms of Sir3-Sir4 interaction and the assembly of a ternary Sir2/Sir3/Sir4 complex that are essential for epigenetic control of gene expression in S. cerevisiae.
Xu
Rui-Ming
RM
D001665:Binding Sites; D015966:Gene Expression Regulation, Fungal; D017434:Protein Structure, Tertiary; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D038281:Silent Information Regulator Proteins, Saccharomyces cerevisiae / Q000737:chemistry* / Q000378:metabolism
C084122:SIR3 protein, S cerevisiae; C061573:SIR4 protein, S cerevisiae; D038281:Silent Information Regulator Proteins, Saccharomyces cerevisiae