NMR assignments and histone specificity of the ING2 PHD finger

被引：7

作者：

Pena, Pedro V. ^{[1
]}

Musselman, Catherine A. ^{[1
]}

Kuo, Alex J. ^{[2
]}

Gozani, Or ^{[2
]}

Kutateladze, Tatiana G. ^{[1
]}

机构：

[1] Univ Colorado Denver, Sch Med, Dept Pharmacol, Aurora, CO 80045 USA

[2] Stanford Univ, Dept Biol Sci, Stanford, CA 94305 USA

来源：

MAGNETIC RESONANCE IN CHEMISTRY | 2009年 / 47卷 / 04期

基金：

美国国家卫生研究院;

关键词：

NMR; histone; chromatin; PHD finger; resonance assignment; TUMOR-SUPPRESSOR; STRUCTURAL BASIS; BINDING MODULES; LYSINE-4; METHYLATION; MOLECULAR-BASIS; H3; PROTEINS; RECOGNITION; SPECTROSCOPY; CHROMODOMAIN;

D O I：

10.1002/mrc.2390

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

The ING2 plant homeodomain (PHD) finger is recruited to the nucleosome through specific binding to histone H3 trimethylated at lysine 4 (H3K4me3). Here, we describe backbone and side chain assignments of the ING2 PHD finger, analyze its binding to the unmodified and modified histone and p53 peptides, and map the histone H3 and H3K4me3 binding sites based on chemical shift perturbation analysis. Copyright (c) 2009 John Wiley & Sons, Ltd.

引用

页码：352 / 358

页数：7

共 49 条

[1] THE PHD FINGER - IMPLICATIONS FOR CHROMATIN-MEDIATED TRANSCRIPTIONAL REGULATION [J].

AASLAND, R ;

GIBSON, TJ ;

STEWART, AF .

TRENDS IN BIOCHEMICAL SCIENCES, 1995, 20 (02) :56-59

[2] Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain [J].

Bannister, AJ ;

Zegerman, P ;

Partridge, JF ;

Miska, EA ;

Thomas, JO ;

Allshire, RC ;

Kouzarides, T .

NATURE, 2001, 410 (6824) :120-124

[3] Biological functions of the ING family tumor suppressors [J].

Campos, EI ;

Chin, MY ;

Kuo, WH ;

Li, G .

CELLULAR AND MOLECULAR LIFE SCIENCES, 2004, 61 (19-20) :2597-2613

[4] Regulation of p53 activity through lysine methylation [J].

Chuikov, S ;

Kurash, JK ;

Wilson, JR ;

Xiao, B ;

Justin, N ;

Ivanov, GS ;

McKinney, K ;

Tempst, P ;

Prives, C ;

Gamblin, SJ ;

Barlev, NA ;

Reinberg, D .

NATURE, 2004, 432 (7015) :353-360

[5] The ankyrin repeats of G9a and GLP histone methyltransferases are mono- and dimethyllysine binding modules [J].

Collins, Robert E. ;

Northrop, Jeffrey P. ;

Horton, John R. ;

Lee, David Y. ;

Zhang, Xing ;

Stallcup, Michael R. ;

Cheng, Xiaodong .

NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2008, 15 (03) :245-250

[6] NMRPIPE - A MULTIDIMENSIONAL SPECTRAL PROCESSING SYSTEM BASED ON UNIX PIPES [J].

DELAGLIO, F ;

GRZESIEK, S ;

VUISTER, GW ;

ZHU, G ;

PFEIFER, J ;

BAX, A .

JOURNAL OF BIOMOLECULAR NMR, 1995, 6 (03) :277-293

[7] Structure and ligand of a histone acetyltransferase bromodomain [J].

Dhalluin, C ;

Carlson, JE ;

Zeng, L ;

He, C ;

Aggarwal, AK ;

Zhou, MM .

NATURE, 1999, 399 (6735) :491-496

[8] ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation [J].

Doyon, Y ;

Cayrou, C ;

Ullah, M ;

Landry, AJ ;

Côté, V ;

Selleck, W ;

Lane, WS ;

Tan, S ;

Yang, XJ ;

Côté, J .

MOLECULAR CELL, 2006, 21 (01) :51-64

[9] Molecular basis for the discrimination of repressive methyl-lysine marks in histone H3 bv Polvcomb and HP1 chromodomains [J].

Fischle, W ;

Wang, YM ;

Jacobs, SA ;

Kim, YC ;

Allis, CD ;

Khorasanizadeh, S .

GENES & DEVELOPMENT, 2003, 17 (15) :1870-1881

[10] Double chromodomains cooperate to recognize the methylated histone H3 tail [J].

Flanagan, JF ;

Mi, LZ ;

Chruszcz, M ;

Cymborowski, M ;

Clines, KL ;

Kim, YC ;

Minor, W ;

Rastinejad, F ;

Khorasanizadeh, S .

NATURE, 2005, 438 (7071) :1181-1185

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