The histone chaperone sNASP binds a conserved peptide motif within the globular core of histone H3 through its TPR repeats.
Cast your vote
You can rate an item by clicking the amount of stars they wish to award to this item.
When enough users have cast their vote on this item, the average rating will also be shown.
Your vote was cast
Thank you for your feedback
Thank you for your feedback
Singh, Hari R
Ladurner, Andreas G
MetadataShow full item record
AbstractEukaryotic chromatin is a complex yet dynamic structure, which is regulated in part by the assembly and disassembly of nucleosomes. Key to this process is a group of proteins termed histone chaperones that guide the thermodynamic assembly of nucleosomes by interacting with soluble histones. Here we investigate the interaction between the histone chaperone sNASP and its histone H3 substrate. We find that sNASP binds with nanomolar affinity to a conserved heptapeptide motif in the globular domain of H3, close to the C-terminus. Through functional analysis of sNASP homologues we identified point mutations in surface residues within the TPR domain of sNASP that disrupt H3 peptide interaction, but do not completely disrupt binding to full length H3 in cells, suggesting that sNASP interacts with H3 through additional contacts. Furthermore, chemical shift perturbations from(1)H-(15)N HSQC experiments show that H3 peptide binding maps to the helical groove formed by the stacked TPR motifs of sNASP. Our findings reveal a new mode of interaction between a TPR repeat domain and an evolutionarily conserved peptide motif found in canonical H3 and in all histone H3 variants, including CenpA and have implications for the mechanism of histone chaperoning within the cell.
CitationThe histone chaperone sNASP binds a conserved peptide motif within the globular core of histone H3 through its TPR repeats. 2016, 44 (7):3105-17 Nucleic Acids Res.
AffiliationBiomedical Center, Faculty of Medicine, Ludwig-Maximilians-Universit ̈ at München, Großhaderner Strasse 9..
JournalNucleic acids research
The following license files are associated with this item:
- sNASP and ASF1A function through both competitive and compatible modes of histone binding.
- Authors: Bowman A, Koide A, Goodman JS, Colling ME, Zinne D, Koide S, Ladurner AG
- Issue date: 2017 Jan 25
- The human histone chaperone sNASP interacts with linker and core histones through distinct mechanisms.
- Authors: Wang H, Ge Z, Walsh ST, Parthun MR
- Issue date: 2012 Jan
- Nucleosome formation activity of human somatic nuclear autoantigenic sperm protein (sNASP).
- Authors: Osakabe A, Tachiwana H, Matsunaga T, Shiga T, Nozawa RS, Obuse C, Kurumizaka H
- Issue date: 2010 Apr 16
- Solution structure of histone chaperone ANP32B: interaction with core histones H3-H4 through its acidic concave domain.
- Authors: Tochio N, Umehara T, Munemasa Y, Suzuki T, Sato S, Tsuda K, Koshiba S, Kigawa T, Nagai R, Yokoyama S
- Issue date: 2010 Aug 6
- sNASP, a histone H1-specific eukaryotic chaperone dimer that facilitates chromatin assembly.
- Authors: Finn RM, Browne K, Hodgson KC, Ausió J
- Issue date: 2008 Aug