This motif facilitates the formation of heterodimers, which subsequently assemble into a histone octamer, playing a crucial role in the packaging of DNA into nucleosomes within chromatin.
[1] This fold is an ancient and highly conserved structural motif, essential for DNA compaction and regulation across a wide range of species.
The histone fold motif was first discovered in TATA box-binding protein-associated factors, which play a key role in transcription.
[1] The histone fold is typically around 70 amino acids long and is characterized by three alpha helices connected by two short, unstructured loops.
[2] Studies on species like Drosophila have revealed variations in the histone fold motif, particularly in the subunits of transcription initiation factors.