5bt1
histone chaperone Hif1 playing with histone H2A-H2B dimer
Structural highlights
FunctionHIF1_YEAST Histone H3 and H4 specific chaperone component of the nuclear histone acetyltransferase B (HAT-B) complex. Involved in chromatin assembly and telomere silencing.[1] [2] Publication Abstract from PubMedHistone chaperones are critical for guiding specific post-transcriptional modifications of histones, safeguarding the histone deposition (or disassociation) of nucleosome (dis)assembly, and regulating chromatin structures to change gene activities. HAT1-interacting factor 1 (Hif1) has been reported to be an H3-H4 chaperone and to be involved in telomeric silencing and nucleosome (dis)assembly. However, the structural basis for the interaction of Hif1 with histones remains unknown. Here, we report the complex structure of Hif1 binding to H2A-H2B for uncovering the chaperone specificities of Hif1 on binding to both the H2A-H2B dimer and the H3-H4 tetramer. Our findings reveal that Hif1 interacts with the H2A-H2B dimer and the H3-H4 tetramer via distinct mechanisms, suggesting that Hif1 is a pivotal scaffold on alternate binding of H2A-H2B and H3-H4. These specificities are conserved features of the Sim3-Hif1-NASP interrupted tetratricopeptide repeat proteins, which provide clues for investigating their potential roles in nucleosome (dis)assembly. Structural Insights into the Association of Hif1 with Histones H2A-H2B Dimer and H3-H4 Tetramer.,Zhang M, Liu H, Gao Y, Zhu Z, Chen Z, Zheng P, Xue L, Li J, Teng M, Niu L Structure. 2016 Oct 4;24(10):1810-1820. doi: 10.1016/j.str.2016.08.001. Epub 2016, Sep 8. PMID:27618665[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||
