Pulling a single chromatin fiber reveals the forces that maintain its higher-order structure

被引:377
作者
Cui, Y
Bustamante, C
机构
[1] Univ Calif Berkeley, Dept Mol & Cell Biol, Berkeley, CA 94720 USA
[2] Univ Calif Berkeley, Dept Phys, Berkeley, CA 94720 USA
[3] Lawrence Berkeley Lab, Phys Biosci Div, Berkeley, CA 94720 USA
关键词
D O I
10.1073/pnas.97.1.127
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Single chicken erythrocyte chromatin fibers were stretched and released at room temperature with force-measuring laser tweezers. In low ionic strength, the stretch-release curves reveal a process of continuous deformation with little or no internucleosomal attraction. A persistence length of 30 nm and a stretch modulus of approximate to 5 pN is determined for the fibers. At forces of 20 pN and higher, the fibers are modified irreversibly, probably through the mechanical removal of the histone cores from native chromatin. In 40-150 mM NaCl, a distinctive condensation-decondensation transition appears between 5 and 6 pN. corresponding to an internucleosomal attraction energy of approximate to 2.0 kcal/mol per nucleosome. Thus, in physiological ionic strength the fibers possess a dynamic structure in which the fiber locally interconverting between "open" and "closed" states because of thermal fluctuations.
引用
收藏
页码:127 / 132
页数:6
相关论文
共 35 条
[1]   THE NUCLEOSOMAL CORE HISTONE OCTAMER AT 3.1-A RESOLUTION - A TRIPARTITE PROTEIN ASSEMBLY AND A LEFT-HANDED SUPERHELIX [J].
ARENTS, G ;
BURLINGAME, RW ;
WANG, BC ;
LOVE, WE ;
MOUDRIANAKIS, EN .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1991, 88 (22) :10148-10152
[2]   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
[3]   CHROMATIN CONFORMATION AND SALT-INDUCED COMPACTION - 3-DIMENSIONAL STRUCTURAL INFORMATION FROM CRYOELECTRON MICROSCOPY [J].
BEDNAR, J ;
HOROWITZ, RA ;
DUBOCHET, J ;
WOODCOCK, CL .
JOURNAL OF CELL BIOLOGY, 1995, 131 (06) :1365-1376
[4]   ENTROPIC ELASTICITY OF LAMBDA-PHAGE DNA [J].
BUSTAMANTE, C ;
MARKO, JF ;
SIGGIA, ED ;
SMITH, S .
SCIENCE, 1994, 265 (5178) :1599-1600
[5]   Visualization and analysis of chromatin by scanning force microscopy [J].
Bustamante, C ;
Zuccheri, G ;
Leuba, SH ;
Yang, GL ;
Samori, B .
METHODS, 1997, 12 (01) :73-83
[6]   Dinucleosomes show compaction by ionic strength, consistent with bending of linker DNA [J].
Butler, PJG ;
Thomas, JO .
JOURNAL OF MOLECULAR BIOLOGY, 1998, 281 (03) :401-407
[7]   DNA AT THE ENTRY-EXIT OF THE NUCLEOSOME OBSERVED BY CRYOELECTRON MICROSCOPY [J].
FURRER, P ;
BEDNAR, J ;
DUBOCHET, J ;
HAMICHE, A ;
PRUNELL, A .
JOURNAL OF STRUCTURAL BIOLOGY, 1995, 114 (03) :177-183
[8]   Linker histone-dependent DNA structure in linear mononucleosomes [J].
Hamiche, A ;
Schultz, P ;
Ramakrishnan, V ;
Oudet, P ;
Prunell, A .
JOURNAL OF MOLECULAR BIOLOGY, 1996, 257 (01) :30-42
[9]   THE 3-DIMENSIONAL ARCHITECTURE OF CHROMATIN IN-SITU - ELECTRON TOMOGRAPHY REVEALS FIBERS COMPOSED OF A CONTINUOUSLY VARIABLE ZIGZAG NUCLEOSOMAL RIBBON [J].
HOROWITZ, RA ;
AGARD, DA ;
SEDAT, JW ;
WOODCOCK, CL .
JOURNAL OF CELL BIOLOGY, 1994, 125 (01) :1-10
[10]  
KATRITCH V, 1999, IN PRESS J MOL BIOL