Structural highlights
Publication Abstract from PubMed
Yeast Hif1, a homologue of human nuclear autoantigenic sperm protein (NASP), is a histone chaperone that involved in various protein complexes modifying histones during telomeric silencing and chromatin reassembly. For elucidating the structural basis of Hif1, here, we present crystal structure of Hif1 that consists of a superhelixed TPR domain and an extended acid loop covering the rear of TPR domain, which represents typical characters of SHNi-TPR (Sim3-Hif1-NASP interrupted TPR) proteins. Our binding assay indicates that Hif1 could bind to histone octamer via histone H3 and H4. However, the acid loop is crucial for the binding of histones while it may also change the conformation of TPR groove. By binding to core histone complex Hif1 may recruit functional protein complexes to modify histones during chromatin reassembly.
Structural insights into yeast histone chaperone Hif1: a scaffold protein recruiting protein complexes to core histones.,Liu H, Zhang M, He W, Zhu Z, Teng M, Gao Y, Niu L Biochem J. 2014 Jun 20. PMID:24946827[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Liu H, Zhang M, He W, Zhu Z, Teng M, Gao Y, Niu L. Structural insights into yeast histone chaperone Hif1: a scaffold protein recruiting protein complexes to core histones. Biochem J. 2014 Jun 20. PMID:24946827 doi:http://dx.doi.org/10.1042/BJ20131640
