4NQ0

Structural insights into yeast histone chaperone Hif1: a scaffold protein recruiting protein complexes to core histones

Summary for 4NQ0

• Entry DOI: 10.2210/pdb4nq0/pdb
• Descriptor: HAT1-interacting factor 1 (2 entities in total)
• Functional Keywords: tpr, nasp homologue, shni-tpr, mediating protein-protein interactions, histone chaperone, nucleus, chaperone
• Biological source: Saccharomyces cerevisiae (Baker's yeast)
• Cellular location: Nucleus : Q12373
• Total number of polymer chains: 1
• Total formula weight: 44553.19

Authors

Liu, H.,Zhang, M.,He, W.,Zhu, Z.,Teng, M.,Gao, Y.,Niu, L. (deposition date: 2013-11-23, release date: 2014-07-16, Last modification date: 2024-03-20)

Primary citation

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., 462:465-473, 2014

PubMed Abstract: Yeast Hif1 [Hat1 (histone acetyltransferase 1)-interacting factor], a homologue of human NASP (nuclear autoantigenic sperm protein), is a histone chaperone that is involved in various protein complexes which modify histones during telomeric silencing and chromatin reassembly. For elucidating the structural basis of Hif1, in the present paper we demonstrate the crystal structure of Hif1 consisting of a superhelixed TPR (tetratricopeptide repeat) domain and an extended acid loop covering the rear of TPR domain, which represent typical characteristics of SHNi-TPR [Sim3 (start independent of mitosis 3)-Hif1-NASP interrupted TPR] proteins. Our binding assay indicates that Hif1 could bind to the histone octamer via histones H3 and H4. The acid loop is shown to be crucial for the binding of histones and may also change the conformation of the TPR groove. By binding to the core histone complex Hif1 may recruit functional protein complexes to modify histones during chromatin reassembly.

PubMed: 24946827
DOI: 10.1042/BJ20131640

Experimental method

X-RAY DIFFRACTION (2.1 Å)