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histone chaperone RTT106, regulator of Ty1 transposition protein 106; N-terminal homodimerization domain This cd includes the N-terminal homodimerization domain of Saccharomyces cerevisiae Rtt106, a histone chaperone. In addition to this domain, Rtt106 contains two C-terminal pleckstrin-homology (PH) domains. The acetylation of lysine 56 in histone H3 (H3K56ac) is implicated in regulating nucleosome disassembly during gene transcription, and nucleosome assembly during DNA replication and repair. Rtt106 has been shown to aid in the efficient deposition of newly synthesized H3K56ac onto replicating DNA. The interaction of Rtt106 with (H3-H4)2, most likely in the form of a (H3-H4)2 tetramer, is important for gene silencing and for the DNA damage response. Data supports a combinatorial interaction: this N-terminal domain homodimerizes and intercalates between the two H3-H4 components of the (H3-H4)2 tetramer, independent of acetylation, and the two double PH domains bind the K56-containing region of H3. Acetylation of K56 increases the affinity of the interaction. Rtt106 also interacts with both the SWI/SNF and RSC chromatin remodeling complexes and is involved in their cell-cycle dependent recruitment to histone gene pairs regulated by the HIR co-repressor complex (HTA1-HTB1, HHT1-HHF1, and HHT2-HHF2). Saccharomyces cerevisiae Rtt106 also plays a role in a role in regulating Ty1 transposition. |
Jiyao W et al.(2023). "The conserved domain database in 2023.",