Histones H3 and H4 chaperone involved in the nucleosome formation and heterochromatin silencing. Required for the deposition of H3K56ac-carrying H3-H4 complex onto newly-replicated DNA. Plays a role in the transcriptional regulation of the cell-cycle dependent histone genes by directly recruiting the SWI/SNF and RSC chromatin remodeling complexes to the histone genes in a cell cycle dependent manner. In cooperation with HIR and ASF1, creates a repressive structure at the core histone gene promoter and contributes to their repression outside of S phase. Involved in regulation of Ty1 transposition. Homodimers (via the N-terminal domain) (PubMed:22307274). Interacts with the SWI/SNF complex (PubMed:21698254). Interacts with the RSC complex (PubMed:21698254). Interacts with the HIR complex (PubMed:21698254, PubMed:19683497). Interacts with the CAF-1 complex (PubMed:19683497). Interacts with RLF2 (PubMed:16157874). Interacts with SIR4 (PubMed:17410207). Interacts with YTA7 (PubMed:22156209). Interacts with CAC2 (PubMed:19683497). Interacts with HPC2 (PubMed:19683497). Interacts with HIR2 (PubMed:19683497). Interacts with MSI1 (PubMed:19683497). Interacts with HIR1 (PubMed:19683497). Interacts with histone H3 (PubMed:16157874, PubMed:20007951, PubMed:20188666, PubMed:21444721, PubMed:22307274). Interacts with histone H4 (PubMed:16157874, PubMed:20007951, PubMed:21444721, PubMed:22307274). Localizes to the promoter region of histones HTA1-HTB1, HHT1-HHF1, and HHT2-HHF2,. The N-ter domain (residues 1-67) homodimerizes and interacts with H3-H4 independently of acetylation while the double pleckstrin-homology (PH) domain (residues 68-301) binds the 'Lys-56'-containing region of H3. Decreases nucleosomal density (PubMed:25406467, PubMed:19683497). Increases HTA1 RNA level; simultaneous disruption RTT109 alleviates the effect (PubMed:22156209, PubMed:19683497). Present with 11100 molecules/cell in log phase SD medium. Belongs to the RTT106 family.