FAPP1 Associated Protein 1 (FASP1)

FASP1, was obtained by using yeast two-hybrid system. The interaction between pp5644 and FASP1 was experimentally confirmed by GST pull-down assay In vitro and co-immunoprecipitation assay in vivo. Co-localization of pp5644 and FASP1 in cytoplasm in Hela cells could further support the interaction. Based on the experimental results, it is suggested that pp5644 physically bind to FASP1 and the biological significance of this kind of interaction in vivo is discussed.

Tricostatin A, an inhibitor to histone deacetylase, suppresses the loss of CENP-A recruitment to centromeres in hMis18alpha RNAi cells. Telophase centromere chromatin may be primed or licensed by the hMis18 complex and RbAp46/48 to recruit CENP-A through regulating the acetylation status in the centromere.