Structural plasticity of single chromatin fibers revealed by torsional manipulation

被引:124
作者
Bancaud, A
Silva, NCE
Barbi, M
Wagner, G
Allemand, JF
Mozziconacci, J
Lavelle, C
Croquette, V
Victor, JM
Prunell, A
Viovy, JL [1 ]
机构
[1] Inst Curie, UMR 168, F-75231 Paris, France
[2] Inst Jacques Monod, UMR 7592, F-75251 Paris 05, France
[3] Lab Phys Theor Mat Condensee, UMR 7600, F-75252 Paris 05, France
[4] Lab Phys Stat, UMR 8549, F-75231 Paris 05, France
关键词
D O I
10.1038/nsmb1087
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Magnetic tweezers were used to study the mechanical response under torsion of single nucleosome arrays reconstituted on tandem repeats of 5S positioning sequences. Regular arrays are extremely resilient and can reversibly accommodate a large amount of supercoiling without much change in length. This behavior is quantitatively described by a molecular model of the chromatin three-dimensional architecture. In this model, we assume the existence of a dynamic equilibrium between three conformations of the nucleosome, corresponding to different crossing statuses of the entry/exit DNAs ( positive, null or negative, respectively). Torsional strain displaces that equilibrium, leading to an extensive reorganization of the fiber's architecture. The model explains a number of long-standing topological questions regarding DNA in chromatin and may provide the basis to better understand the dynamic binding of chromatin-associated proteins.
引用
收藏
页码:444 / 450
页数:7
相关论文
共 43 条
[1]   Preferential interaction of the core histone tail domains with linker DNA [J].
Angelov, D ;
Vitolo, JM ;
Mutskov, V ;
Dimitrov, S ;
Hayes, JJ .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2001, 98 (12) :6599-6604
[2]  
[Anonymous], CHROMATIN STRUCTURE
[3]   How the chromatin fiber deals with topological constraints [J].
Barbi, M ;
Mozziconacci, J ;
Victor, JM .
PHYSICAL REVIEW E, 2005, 71 (03)
[4]   Nucleosomes, linker DNA, and linker histone form a unique structural motif that directs the higher-order folding and compaction of chromatin [J].
Bednar, J ;
Horowitz, RA ;
Grigoryev, SA ;
Carruthers, LM ;
Hansen, JC ;
Koster, AJ ;
Woodcock, CL .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (24) :14173-14178
[5]   Chromatin:: A tunable spring at work inside chromosomes -: art. no. 051921 [J].
Ben-Haïm, E ;
Lesne, A ;
Victor, JM .
PHYSICAL REVIEW E, 2001, 64 (05) :19-051921
[6]   Elasticity model of a supercoiled DNA molecule [J].
Bouchiat, C ;
Mezard, M .
PHYSICAL REVIEW LETTERS, 1998, 80 (07) :1556-1559
[7]   Mechanical disruption of individual nucleosomes reveals a reversible multistage release of DNA [J].
Brower-Toland, BD ;
Smith, CL ;
Yeh, RC ;
Lis, JT ;
Peterson, CL ;
Wang, MD .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (04) :1960-1965
[8]   The dynamics of histone H1 function in chromatin [J].
Bustin, M ;
Catez, F ;
Lim, JH .
MOLECULAR CELL, 2005, 17 (05) :617-620
[9]   Network of dynamic interactions between histone H1 and high-mobility-group proteins in chromatin [J].
Catez, F ;
Yang, H ;
Tracey, KJ ;
Reeves, R ;
Misteli, T ;
Bustin, M .
MOLECULAR AND CELLULAR BIOLOGY, 2004, 24 (10) :4321-4328
[10]   EFFECT OF POSITIVE SUPERCOILING ON DNA COMPACTION BY NUCLEOSOME CORES [J].
CLARK, DJ ;
GHIRLANDO, R ;
FELSENFELD, G ;
EISENBERG, H .
JOURNAL OF MOLECULAR BIOLOGY, 1993, 234 (02) :297-301