scholarly journals Structural basis for site-specific reading of unmodified R2 of histone H3 tail by UHRF1 PHD finger

Cell Research ◽  
2011 ◽  
Vol 21 (9) ◽  
pp. 1379-1382 ◽  
Author(s):  
Chengkun Wang ◽  
Jie Shen ◽  
Zhongzheng Yang ◽  
Ping Chen ◽  
Bin Zhao ◽  
...  
Keyword(s):  
Histone H3 ◽  
Structural Basis ◽  
Site Specific ◽  
Phd Finger ◽  
Specific Reading

scholarly journals Structural basis of molecular recognition of helical histone H3 tail by PHD finger domains

2017 ◽  
Vol 474 (10) ◽  
pp. 1633-1651 ◽  
Author(s):  
Alessio Bortoluzzi ◽  
Anastasia Amato ◽  
Xavier Lucas ◽  
Manuel Blank ◽  
Alessio Ciulli
Keyword(s):  
Secondary Structure ◽  
Molecular Recognition ◽  
Histone H3 ◽  
Structural Basis ◽  
Bioinformatics Analyses ◽  
Histone Tails ◽  
Interacting Protein ◽  
Post Translational Modifications ◽  
Phd Finger ◽  
Additional Layer

The plant homeodomain (PHD) fingers are among the largest family of epigenetic domains, first characterized as readers of methylated H3K4. Readout of histone post-translational modifications by PHDs has been the subject of intense investigation; however, less is known about the recognition of secondary structure features within the histone tail itself. We solved the crystal structure of the PHD finger of the bromodomain adjacent to zinc finger 2A [BAZ2A, also known as TIP5 (TTF-I/interacting protein 5)] in complex with unmodified N-terminal histone H3 tail. The peptide is bound in a helical folded-back conformation after K4, induced by an acidic patch on the protein surface that prevents peptide binding in an extended conformation. Structural bioinformatics analyses identify a conserved Asp/Glu residue that we name ‘acidic wall’, found to be mutually exclusive with the conserved Trp for K4Me recognition. Neutralization or inversion of the charges at the acidic wall patch in BAZ2A, and homologous BAZ2B, weakened H3 binding. We identify simple mutations on H3 that strikingly enhance or reduce binding, as a result of their stabilization or destabilization of H3 helicity. Our work unravels the structural basis for binding of the helical H3 tail by PHD fingers and suggests that molecular recognition of secondary structure motifs within histone tails could represent an additional layer of regulation in epigenetic processes.

scholarly journals Structure and Site-Specific Recognition of Histone H3 by the PHD Finger of Human Autoimmune Regulator

Structure ◽  
2009 ◽  
Vol 17 (5) ◽  
pp. 670-679 ◽  
Author(s):  
Suvobrata Chakravarty ◽  
Lei Zeng ◽  
Ming-Ming Zhou
Keyword(s):  
Histone H3 ◽  
Site Specific ◽  
Phd Finger ◽  
Autoimmune Regulator ◽  
Specific Recognition

scholarly journals Structural Basis of LSD1-CoREST Selectivity in Histone H3 Recognition

2007 ◽  
Vol 282 (28) ◽  
pp. 20070-20074 ◽  
Author(s):  
Federico Forneris ◽  
Claudia Binda ◽  
Antonio Adamo ◽  
Elena Battaglioli ◽  
Andrea Mattevi
Keyword(s):  
Histone H3 ◽  
Structural Basis

scholarly journals Structural basis of recognition and destabilization of the histone H2B ubiquitinated nucleosome by the DOT1L histone H3 Lys79 methyltransferase

2019 ◽  
Vol 33 (11-12) ◽  
pp. 620-625 ◽  
Author(s):  
Seongmin Jang ◽  
Chanshin Kang ◽  
Han-Sol Yang ◽  
Taeyang Jung ◽  
Hans Hebert ◽  
...  
Keyword(s):  
Histone H3 ◽  
Structural Basis ◽  
Histone H2b

scholarly journals Site-specific Loss of Acetylation upon Phosphorylation of Histone H3

2002 ◽  
Vol 277 (33) ◽  
pp. 29496-29502 ◽  
Author(s):  
Diane G. Edmondson ◽  
Judith K. Davie ◽  
Jenny Zhou ◽  
Banafsheh Mirnikjoo ◽  
Kelly Tatchell ◽  
...  
Keyword(s):  
Histone H3 ◽  
Site Specific ◽  
Specific Loss

scholarly journals Crosstalk between site-specific modifications on p53 and histone H3

Oncogene ◽  
2007 ◽  
Vol 27 (11) ◽  
pp. 1639-1644 ◽  
Author(s):  
L J Warnock ◽  
R Adamson ◽  
C J Lynch ◽  
J Milner
Keyword(s):  
Histone H3 ◽  
Site Specific
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