A common structural theme in histone chaperones mimics interhistone contacts

Trends in Biochemical Sciences

Volumn 38, Issue 7, 2013, Pages 333-336

  Elsässer, Simon J ^a  

^a MRC LABORATORY OF MOLECULAR BIOLOGY   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CENTROMERE PROTEIN A; CHAPERONE; DAXX PROTEIN; HISTONE; HISTONE H3; HISTONE H4; HOLLIDAY JUNCTION RECOGNITION PROTEIN; INTERHISTONE; SUPPRESSOR OF CHROMOSOME MISSEGREGATION; UNCLASSIFIED DRUG;

ALPHA HELIX; ANIMAL; CRYSTAL STRUCTURE; DNA BINDING MOTIF; HUMAN; NONHUMAN; NOTE; NUCLEOSOME; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY; YEAST;

ADAPTOR PROTEINS, SIGNAL TRANSDUCING; AMINO ACID SEQUENCE; ANIMALS; CHROMOSOMAL PROTEINS, NON-HISTONE; CONSERVED SEQUENCE; DNA-BINDING PROTEINS; HISTONE CHAPERONES; HISTONES; HUMANS; NUCLEAR PROTEINS; NUCLEOSOMES; PHYLOGENY; PROTEIN INTERACTION DOMAINS AND MOTIFS; SACCHAROMYCES CEREVISIAE PROTEINS;

EUKARYOTA;

EID: 84879449165     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2013.04.002     Document Type: Note

References (15)

1. Andrews A.J., Luger K. Nucleosome structure(s) and stability: variations on a theme. Annu. Rev. Biophys. 2011, 40:99-117.
2. Hondele M., Ladurner A.G. The chaperone-histone partnership: for the greater good of histone traffic and chromatin plasticity. Curr. Opin. Struct. Biol. 2011, 21:698-708.
3. Elsässer S.J., D'Arcy S. Towards a mechanism for histone chaperones. Biochim. Biophys. Acta 2012, 1819:211-221.
4. Sanchez-Pulido L., et al. Common ancestry of the CENP-A chaperones Scm3 and HJURP. Cell 2009, 137:1173-1174.
5. Hu H., et al. Structure of a CENP-A-histone H4 heterodimer in complex with chaperone HJURP. Genes Dev. 2011, 25:901-906.
6. Zhou Z., et al. Structural basis for recognition of centromere histone variant CenH3 by the chaperone Scm3. Nature 2011, 472:234-237.
7. Cho U-S., Harrison S.C. Recognition of the centromere-specific histone Cse4 by the chaperone Scm3. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:9367-9371.
8. Elsässer S.J., et al. DAXX envelops a histone H3.3-H4 dimer for H3.3-specific recognition. Nature 2012, 491:560-565.
9. Bassett E.A., et al. HJURP uses distinct CENP-A surfaces to recognize and to stabilize CENP-A/histone H4 for centromere assembly. Dev. Cell 2012, 22:749-762.
10. Liu C-P., et al. Structure of the variant histone H3.3-H4 heterodimer in complex with its chaperone DAXX. Nat. Struct. Mol. Biol. 2012, 19:1287-1292.
11. Phansalkar R., et al. Evolutionary insights into the role of the essential centromere protein CAL1 in Drosophila. Chromosome Res. 2012, 20:493-504.
12. Malik H.S., Henikoff S. Major evolutionary transitions in centromere complexity. Cell 2009, 138:1067-1082.
13. Eddy S.R. Accelerated profile HMM searches. PLoS Comput. Biol. 2011, 7:e1002195.
14. English C.M., et al. Structural basis for the histone chaperone activity of Asf1. Cell 2006, 127:495-508.
15. Schuster-Böckler B., et al. HMM logos for visualization of protein families. BMC Bioinformatics 2004, 5:7.