7V1M

Structural basis for the co-chaperone relationship of sNASP and ASF1b

Summary for 7V1M

• Entry DOI: 10.2210/pdb7v1m/pdb
• Descriptor: Histone H3.3, Histone H4, Histone chaperone ASF1B, ... (4 entities in total)
• Functional Keywords: histone chaperone, chaperone
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 8
• Total formula weight: 141969.45

Authors

Bao, H.,Huang, H. (deposition date: 2021-08-04, release date: 2022-04-20, Last modification date: 2023-11-29)

Primary citation

Bao, H.,Carraro, M.,Flury, V.,Liu, Y.,Luo, M.,Chen, L.,Groth, A.,Huang, H.
NASP maintains histone H3-H4 homeostasis through two distinct H3 binding modes.
Nucleic Acids Res., 50:5349-5368, 2022

PubMed Abstract: Histone chaperones regulate all aspects of histone metabolism. NASP is a major histone chaperone for H3-H4 dimers critical for preventing histone degradation. Here, we identify two distinct histone binding modes of NASP and reveal how they cooperate to ensure histone H3-H4 supply. We determine the structures of a sNASP dimer, a complex of a sNASP dimer with two H3 α3 peptides, and the sNASP-H3-H4-ASF1b co-chaperone complex. This captures distinct functionalities of NASP and identifies two distinct binding modes involving the H3 α3 helix and the H3 αN region, respectively. Functional studies demonstrate the H3 αN-interaction represents the major binding mode of NASP in cells and shielding of the H3 αN region by NASP is essential in maintaining the H3-H4 histone soluble pool. In conclusion, our studies uncover the molecular basis of NASP as a major H3-H4 chaperone in guarding histone homeostasis.

PubMed: 35489058
DOI: 10.1093/nar/gkac303

Experimental method

X-RAY DIFFRACTION (2.834 Å)