CENP-C, one of the few known intrinsic proteins of the human centromere, is thought to play structural as well as regulatory roles crucial to proper chromosome segregation and mitotic progression. To further define the functions of CENP-C throughout the cell cycle we have used the yeast interaction trap to identify proteins with which it interacts. One specific CENP-C interactor, which we have named HDaxx, was characterized in detail and found to be homologous to murine Daxx, a protein identified through its ability to bind the death domain of Fas (CD95). The interaction between CENP-C and HDaxx is mediated by the amino-terminal 315 amino acids of CENP-C and the carboxyl-terminal 104 amino acids of HDaxx. This region of Daxx is responsible for binding to death domains of several apoptosis signalling proteins. The biological significance of the interaction between CENP-C and HDaxx was confirmed by immunofluorescence colocalization of these two proteins at discrete spots in the nuclei of some interphase HeLa cells. We discuss the functional implications of the interphase-restricted association of HDaxx with centromeres.
- © 1998 by Company of Biologists