Human SWI/SNF nucleosome remodeling activity is partially inhibited by linker histone H1

被引：69

作者：

Hill, DA ^{[1
]}

Imbalzano, AN ^{[1
]}

机构：

[1] Univ Massachusetts, Sch Med, Dept Cell Biol, Worcester, MA 01655 USA

来源：

BIOCHEMISTRY | 2000年 / 39卷 / 38期

关键词：

D O I：

10.1021/bi001330z

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：

The physical structure and the compact nature of the eukaryotic genome present a functional barrier for any cellular process that requires access to the DNA. The linker histone H1 is intrinsically involved in both the determination of and the stability of higher order chromatin structure. Because histone H1 plays a pivotal role in the structure of chromatin, we investigated the effect of histone H1 on the nucleosome remodeling activity of human SWI/SNF, an ATP-dependent chromatin remodeling complex. The results from both DNase I digestion and restriction endonuclease accessibility assays indicate that the presence of H1 partially inhibits the nucleosome remodeling activity of hSWI/SNF. Neither H1 bound to the nucleosome nor free H1 affected the ATPase activity of hSWI/SNF, suggesting that the observed inhibition of hSWI/SNF nucleosome remodeling activity depends on the structure formed by the addition of H1 to nucleosomes.

引用

页码：11649 / 11656

页数：8

共 68 条

[1] Linker histone protection of chromatosomes reconstituted on 5S rDNA from Xenopus borealis:: a reinvestigation [J].

An, WJ ;

van Holde, K ;

Zlatanova, J .

NUCLEIC ACIDS RESEARCH, 1998, 26 (17) :4042-4046

[2] Linker histone protects linker DNA on only one side of the core particle and in a sequence-dependent manner [J].

An, WJ ;

Leuba, SH ;

van Holde, K ;

Zlatanova, J .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (07) :3396-3401

[3] 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

[4] Linker histones: paradigm lost but questions remain [J].

Belikov, S ;

Karpov, V .

FEBS LETTERS, 1998, 441 (02) :161-164

[5] Functional delineation of three groups of the ATP-dependent family of chromatin remodeling enzymes [J].

Boyer, LA ;

Logie, C ;

Bonte, E ;

Becker, PB ;

Wade, PA ;

Wolffe, AP ;

Wu, C ;

Imbalzano, AN ;

Peterson, CL .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (25) :18864-18870

[6] The yeast SWI-SNF complex facilitates binding of a transcriptional activator to nucleosomal sites in vivo [J].

Burns, LG ;

Peterson, CL .

MOLECULAR AND CELLULAR BIOLOGY, 1997, 17 (08) :4811-4819

[7] A MULTISUBUNIT COMPLEX CONTAINING THE SWI1/ADR6, SWI2/SNF2, SWI3, SNF5, AND SNF6 GENE-PRODUCTS ISOLATED FROM YEAST [J].

CAIRNS, BR ;

KIM, YJ ;

SAYRE, MH ;

LAURENT, BC ;

KORNBERG, RD .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1994, 91 (05) :1950-1954

[8] Linker histones stabilize the intrinsic salt-dependent folding of nucleosomal arrays: Mechanistic ramifications for higher-order chromatin folding [J].

Carruthers, LM ;

Bednar, J ;

Woodcock, CL ;

Hansen, JC .

BIOCHEMISTRY, 1998, 37 (42) :14776-14787

[9] 2 HUMAN HOMOLOGS OF SACCHAROMYCES-CEREVISIAE SW12/SNF2 AND DROSOPHILA-BRAHMA ARE TRANSCRIPTIONAL COACTIVATORS COOPERATING WITH THE ESTROGEN-RECEPTOR AND THE RETINOIC ACID RECEPTOR [J].

CHIBA, H ;

MURAMATSU, M ;

NOMOTO, A ;

KATO, H .

NUCLEIC ACIDS RESEARCH, 1994, 22 (10) :1815-1820

[10] ISWI is an ATP-dependent nucleosome remodeling factor [J].

Corona, DFV ;

Längst, G ;

Clapier, CR ;

Bonte, EJ ;

Ferrari, S ;

Tamkun, JW ;

Becker, PB .

MOLECULAR CELL, 1999, 3 (02) :239-245

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