A chromatin remodelling complex that loads cohesin onto human chromosomes

Mohamed Ali Hakimi, Daniel A. Bochar, John A. Schmiesing, Yuanshu Dong, Orr G. Barak, David W. Spelcher, Kyoko Yokomori, Ramin Shiekhattar

Research output: Contribution to journalArticle

207 Citations (Scopus)

Abstract

Nucleosomal DNA is arranged in a higher-order structure that presents a barrier to most cellular processes involving protein DNA interactions. The cellular machinery involved in sister chromatid cohesion, the cohesin complex, also requires access to the nucleosomal DNA to perform its function in chromosome segregation. The machineries that provide this accessibility are termed chromatin remodelling factors. Here, we report the isolation of a human ISWI (SNF2h)-containing chromatin remodelling complex that encompasses components of the cohesin and NuRD complexes. We show that the hRAD21 subunit of the cohesin complex directly interacts with the ATPase subunit SNF2h. Mapping of hRAD21, SNF2h and Mi2 binding sites by chromatin immunoprecipitation experiments reveals the specific association of these three proteins with human DNA elements containing Alu sequences. We find a correlation between modification of histone tails and association of the SNF2h/cohesin complex with chromatin. Moreover, we show that the association of the cohesin complex with chromatin can be regulated by the state of DNA methylation. Finally, we present evidence pointing to a role for the ATPase activity of SNF2h in the loading of hRAD21 on chromatin.

Original languageEnglish (US)
Pages (from-to)994-998
Number of pages5
JournalNature
Volume418
Issue number6901
DOIs
StatePublished - Aug 29 2002
Externally publishedYes

Fingerprint

Chromatin Assembly and Disassembly
Human Chromosomes
Chromatin
DNA
Adenosine Triphosphatases
Mi-2 Nucleosome Remodeling and Deacetylase Complex
Histone Code
Alu Elements
Chromosome Segregation
Chromatids
Chromatin Immunoprecipitation
DNA Methylation
Tail
Proteins
Binding Sites
cohesins

ASJC Scopus subject areas

  • General

Cite this

Hakimi, M. A., Bochar, D. A., Schmiesing, J. A., Dong, Y., Barak, O. G., Spelcher, D. W., ... Shiekhattar, R. (2002). A chromatin remodelling complex that loads cohesin onto human chromosomes. Nature, 418(6901), 994-998. https://doi.org/10.1038/nature01024

A chromatin remodelling complex that loads cohesin onto human chromosomes. / Hakimi, Mohamed Ali; Bochar, Daniel A.; Schmiesing, John A.; Dong, Yuanshu; Barak, Orr G.; Spelcher, David W.; Yokomori, Kyoko; Shiekhattar, Ramin.

In: Nature, Vol. 418, No. 6901, 29.08.2002, p. 994-998.

Research output: Contribution to journalArticle

Hakimi, MA, Bochar, DA, Schmiesing, JA, Dong, Y, Barak, OG, Spelcher, DW, Yokomori, K & Shiekhattar, R 2002, 'A chromatin remodelling complex that loads cohesin onto human chromosomes', Nature, vol. 418, no. 6901, pp. 994-998. https://doi.org/10.1038/nature01024
Hakimi MA, Bochar DA, Schmiesing JA, Dong Y, Barak OG, Spelcher DW et al. A chromatin remodelling complex that loads cohesin onto human chromosomes. Nature. 2002 Aug 29;418(6901):994-998. https://doi.org/10.1038/nature01024
Hakimi, Mohamed Ali ; Bochar, Daniel A. ; Schmiesing, John A. ; Dong, Yuanshu ; Barak, Orr G. ; Spelcher, David W. ; Yokomori, Kyoko ; Shiekhattar, Ramin. / A chromatin remodelling complex that loads cohesin onto human chromosomes. In: Nature. 2002 ; Vol. 418, No. 6901. pp. 994-998.
@article{5d51a2ddeed84d01a48ed8b5733d1ece,
title = "A chromatin remodelling complex that loads cohesin onto human chromosomes",
abstract = "Nucleosomal DNA is arranged in a higher-order structure that presents a barrier to most cellular processes involving protein DNA interactions. The cellular machinery involved in sister chromatid cohesion, the cohesin complex, also requires access to the nucleosomal DNA to perform its function in chromosome segregation. The machineries that provide this accessibility are termed chromatin remodelling factors. Here, we report the isolation of a human ISWI (SNF2h)-containing chromatin remodelling complex that encompasses components of the cohesin and NuRD complexes. We show that the hRAD21 subunit of the cohesin complex directly interacts with the ATPase subunit SNF2h. Mapping of hRAD21, SNF2h and Mi2 binding sites by chromatin immunoprecipitation experiments reveals the specific association of these three proteins with human DNA elements containing Alu sequences. We find a correlation between modification of histone tails and association of the SNF2h/cohesin complex with chromatin. Moreover, we show that the association of the cohesin complex with chromatin can be regulated by the state of DNA methylation. Finally, we present evidence pointing to a role for the ATPase activity of SNF2h in the loading of hRAD21 on chromatin.",
author = "Hakimi, {Mohamed Ali} and Bochar, {Daniel A.} and Schmiesing, {John A.} and Yuanshu Dong and Barak, {Orr G.} and Spelcher, {David W.} and Kyoko Yokomori and Ramin Shiekhattar",
year = "2002",
month = "8",
day = "29",
doi = "10.1038/nature01024",
language = "English (US)",
volume = "418",
pages = "994--998",
journal = "Nature",
issn = "0028-0836",
publisher = "Nature Publishing Group",
number = "6901",

}

TY - JOUR

T1 - A chromatin remodelling complex that loads cohesin onto human chromosomes

AU - Hakimi, Mohamed Ali

AU - Bochar, Daniel A.

AU - Schmiesing, John A.

AU - Dong, Yuanshu

AU - Barak, Orr G.

AU - Spelcher, David W.

AU - Yokomori, Kyoko

AU - Shiekhattar, Ramin

PY - 2002/8/29

Y1 - 2002/8/29

N2 - Nucleosomal DNA is arranged in a higher-order structure that presents a barrier to most cellular processes involving protein DNA interactions. The cellular machinery involved in sister chromatid cohesion, the cohesin complex, also requires access to the nucleosomal DNA to perform its function in chromosome segregation. The machineries that provide this accessibility are termed chromatin remodelling factors. Here, we report the isolation of a human ISWI (SNF2h)-containing chromatin remodelling complex that encompasses components of the cohesin and NuRD complexes. We show that the hRAD21 subunit of the cohesin complex directly interacts with the ATPase subunit SNF2h. Mapping of hRAD21, SNF2h and Mi2 binding sites by chromatin immunoprecipitation experiments reveals the specific association of these three proteins with human DNA elements containing Alu sequences. We find a correlation between modification of histone tails and association of the SNF2h/cohesin complex with chromatin. Moreover, we show that the association of the cohesin complex with chromatin can be regulated by the state of DNA methylation. Finally, we present evidence pointing to a role for the ATPase activity of SNF2h in the loading of hRAD21 on chromatin.

AB - Nucleosomal DNA is arranged in a higher-order structure that presents a barrier to most cellular processes involving protein DNA interactions. The cellular machinery involved in sister chromatid cohesion, the cohesin complex, also requires access to the nucleosomal DNA to perform its function in chromosome segregation. The machineries that provide this accessibility are termed chromatin remodelling factors. Here, we report the isolation of a human ISWI (SNF2h)-containing chromatin remodelling complex that encompasses components of the cohesin and NuRD complexes. We show that the hRAD21 subunit of the cohesin complex directly interacts with the ATPase subunit SNF2h. Mapping of hRAD21, SNF2h and Mi2 binding sites by chromatin immunoprecipitation experiments reveals the specific association of these three proteins with human DNA elements containing Alu sequences. We find a correlation between modification of histone tails and association of the SNF2h/cohesin complex with chromatin. Moreover, we show that the association of the cohesin complex with chromatin can be regulated by the state of DNA methylation. Finally, we present evidence pointing to a role for the ATPase activity of SNF2h in the loading of hRAD21 on chromatin.

UR - http://www.scopus.com/inward/record.url?scp=0037194787&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037194787&partnerID=8YFLogxK

U2 - 10.1038/nature01024

DO - 10.1038/nature01024

M3 - Article

VL - 418

SP - 994

EP - 998

JO - Nature

JF - Nature

SN - 0028-0836

IS - 6901

ER -