Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2016 May;26(5):629-32.
doi: 10.1038/cr.2016.49. Epub 2016 Apr 22.

YEATS2 is a selective histone crotonylation reader

Dan Zhao  1   2 , Haipeng Guan  1 , Shuai Zhao  1 , Wenyi Mi  3 , Hong Wen  3 , Yuanyuan Li  1   4 , Yingming Zhao  5 , C David Allis  6 , Xiaobing Shi  3   7 , Haitao Li  1   8
Affiliations

YEATS2 is a selective histone crotonylation reader

Dan Zhao et al. Cell Res. 2016 May.
No abstract available

PubMed Disclaimer

Figures

Figure 1
Figure 1
The YEATS domain of YEATS2 is a selective reader of H3K27cr. (A) Domain architecture of the YEATS2 protein. (B) Chemical structure of different acyl groups (abbreviations correspond to data shown in D). (C) Representative peptide array results for the YEATS domain of YEATS2 (full view of the array is shown in Supplementary information, Figure S1). (D) ITC fitting curves of the YEATS domain of YEATS2 titrated by a series of H31-34 peptides with acylations or trimethyclation (me3) on K27. (E) ITC fitting curves of YEATS2 titrated by a series of crotonylated histone peptides. (F) Overall structure of YEATS2201-332 bound to the H324-31K27cr peptide in ribbon view (left) and space-filling-surface view color-coded by electrostatic potential ranging from −10 to 10 kT/e (right). YEATS2201-332 (light green) is shown as ribbons, and the histone H3 peptide (yellow) is depicted as sticks. Purple mesh: Fo-Fc omit map around H324-31K27cr peptide contoured at 2.0 σ level. Middle, close-up view of the Kcr-sandwiching pocket; interplanar distances are labeled in the unit of angstrom. (G) The orientation of the H3 peptide bound to the YEATS domain. Upper, the YEATS domain of AF9 bound to the H3K9ac peptide (PDB ID: 4TMP); lower, the YEATS domain of YEATS2 bound to the H3K27cr peptide; bottom, sequence alignment around H3K9 and H3K27 sites. The consensus “ARKS” motif is highlighted in red. (H) Hydrogen bonding network between H3K27cr peptide and YEATS2. Hydrogen bonds are shown as pink dashes. Key residues of YEATS2 are depicted as cyan sticks and labeled black; the H3 peptide is shown as yellow sticks and labeled red. (I) ITC titration fitting curves of binding of YEATS2 YEATS mutants with the H315-39K27cr peptide. (J) Comparison of the acyl-binding pockets of AF9 and YEATS2. Left, H3K9ac in AF9 (PDB ID: 4TMP); right, H3K27cr in YEATS2. (K) Sequence alignment of the acyl-binding pocket among YEATS proteins. S230 of YEATS2 is indicated with a red arrowhead.
See this image and copyright information in PMC

Similar articles

See all similar articles

Cited by

See all "Cited by" articles

References

    1. Tan M, Luo H, Lee S, et al. Cell 2011; 146:1016–1028. - PMC - PubMed
    1. Montellier E, Rousseaux S, Zhao Y, et al. Bioessays 2012; 34:187–193. - PubMed
    1. Flynn EM, Huang OW, Poy F, et al. Structure 2015; 23:1801–1814. - PubMed
    1. Wang YL, Faiola F, Xu M, et al. J Biol Chem 2008; 283:33808–33815. - PMC - PubMed
    1. Orpinell M, Fournier M, Riss A, et al. EMBO J 2010; 29:2381–2394. - PMC - PubMed

Publication types