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Comment
. 2011 Aug 30;108(35):E596; author reply E597.
doi: 10.1073/pnas.1109548108. Epub 2011 Aug 15.

Structure of the budding yeast Saccharomyces cerevisiae centromeric histones Cse4-H4 complexed with the chaperone Scm3

Hanqiao Feng, Zheng Zhou, Bing-Rui Zhou, Yawen Bai
Comment

Structure of the budding yeast Saccharomyces cerevisiae centromeric histones Cse4-H4 complexed with the chaperone Scm3

Hanqiao Feng et al. Proc Natl Acad Sci U S A. .
No abstract available

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Fig. 1.
Fig. 1.
Identification of disordered N-terminal regions of Scm3 and H4 in the three-chain Scm3–Cse4–H4 complexes at pH 5.4 and 22 °C. The Cα chemical shift deviations from corresponding random coil values for the N-terminal region of Scm3 (Upper) and the N-terminal region of H4 (Lower) in the three-chain Sc Scm366–169–Cse4150–228–H41–103 and Scm384–169–Cse4150–228–H41–103 complexes, respectively, are shown. The dashed lines indicate the values of 1 and −1. For residues in β-strands, the values should be below −1. For residues in α-helices, the values should be above 1. The open rectangular bars indicate the corresponding regions of the β-hairpin in the Kl Scm3 and helix I of the Kl H4. Residues 31–41 correspond to helix I of H4 in the histone fold. Residues 1–24 in H4 are in the disordered N-terminal tail, serving as an internal reference.
See this image and copyright information in PMC

Comment on

References

    1. Cho U-S, Harrison SC. Recognition of the centromere-specific histone Cse4 by the chaperone Scm3. Proc Natl Acad Sci USA. 2011;108:9367–9371. - PMC - PubMed
    1. Zhou Z, et al. Structural basis for recognition of centromere histone variant CenH3 by the chaperone Scm3. Nature. 2011;472:234–237. - PMC - PubMed

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