USF1 recruits histone modification complexes and is critical for maintenance of a chromatin barrier

Suming Huang, Xingguo Li, Timur M. Yusufzai, Yi Qiu, Gary Felsenfeld

Research output: Contribution to journalArticle

90 Citations (Scopus)

Abstract

The insulator element at the 5′ end of the chicken β-globin locus acts as a barrier, protecting transgenes against silencing effects of adjacent heterochromatin. We showed earlier that the transcription factor USF1 binds within the insulator and that this site is important for generating in adjacent nucleosomes histone modifications associated with active chromatin and, by inference, with barrier function. To understand the mechanism of USF1 action, we have characterized USF1-containing complexes. USF1 interacts directly with the histone H4R3-specific methyltransferase PRMT1. USF1, PRMT1, and the histone acetyltransferases (HATs) PCAF and SRC-1 form a complex with both H4R3 histone methyltransferase and HAT activities. Small interfering RNA downregulation of USF1 results in localized loss of H4R3 methylation, and other histone modifications associated with euchromatin, at the insulator. A dominant negative peptide that interferes with USF1 binding to DNA causes silencing of an insulated reporter construct, indicating abolition of barrier function. These results show that USF1 plays a direct role in maintaining the barrier, supporting a model in which the insulator works as a barrier by maintaining a local environment of active chromatin.

Original languageEnglish (US)
Pages (from-to)7991-8002
Number of pages12
JournalMolecular and cellular biology
Volume27
Issue number22
DOIs
StatePublished - Nov 1 2007

Fingerprint

Histone Code
Histone Acetyltransferases
Chromatin
Insulator Elements
Maintenance
Euchromatin
Globins
Heterochromatin
Nucleosomes
Methyltransferases
Transgenes
Histones
Methylation
Small Interfering RNA
Chickens
Transcription Factors
Down-Regulation
Peptides
DNA

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

Cite this

Huang, Suming ; Li, Xingguo ; Yusufzai, Timur M. ; Qiu, Yi ; Felsenfeld, Gary. / USF1 recruits histone modification complexes and is critical for maintenance of a chromatin barrier. In: Molecular and cellular biology. 2007 ; Vol. 27, No. 22. pp. 7991-8002.
@article{fe869bd11c524ec5aaa762eae089a9a3,
title = "USF1 recruits histone modification complexes and is critical for maintenance of a chromatin barrier",
abstract = "The insulator element at the 5′ end of the chicken β-globin locus acts as a barrier, protecting transgenes against silencing effects of adjacent heterochromatin. We showed earlier that the transcription factor USF1 binds within the insulator and that this site is important for generating in adjacent nucleosomes histone modifications associated with active chromatin and, by inference, with barrier function. To understand the mechanism of USF1 action, we have characterized USF1-containing complexes. USF1 interacts directly with the histone H4R3-specific methyltransferase PRMT1. USF1, PRMT1, and the histone acetyltransferases (HATs) PCAF and SRC-1 form a complex with both H4R3 histone methyltransferase and HAT activities. Small interfering RNA downregulation of USF1 results in localized loss of H4R3 methylation, and other histone modifications associated with euchromatin, at the insulator. A dominant negative peptide that interferes with USF1 binding to DNA causes silencing of an insulated reporter construct, indicating abolition of barrier function. These results show that USF1 plays a direct role in maintaining the barrier, supporting a model in which the insulator works as a barrier by maintaining a local environment of active chromatin.",
author = "Suming Huang and Xingguo Li and Yusufzai, {Timur M.} and Yi Qiu and Gary Felsenfeld",
year = "2007",
month = "11",
day = "1",
doi = "10.1128/MCB.01326-07",
language = "English (US)",
volume = "27",
pages = "7991--8002",
journal = "Molecular and Cellular Biology",
issn = "0270-7306",
publisher = "American Society for Microbiology",
number = "22",

}

USF1 recruits histone modification complexes and is critical for maintenance of a chromatin barrier. / Huang, Suming; Li, Xingguo; Yusufzai, Timur M.; Qiu, Yi; Felsenfeld, Gary.

In: Molecular and cellular biology, Vol. 27, No. 22, 01.11.2007, p. 7991-8002.

Research output: Contribution to journalArticle

TY - JOUR

T1 - USF1 recruits histone modification complexes and is critical for maintenance of a chromatin barrier

AU - Huang, Suming

AU - Li, Xingguo

AU - Yusufzai, Timur M.

AU - Qiu, Yi

AU - Felsenfeld, Gary

PY - 2007/11/1

Y1 - 2007/11/1

N2 - The insulator element at the 5′ end of the chicken β-globin locus acts as a barrier, protecting transgenes against silencing effects of adjacent heterochromatin. We showed earlier that the transcription factor USF1 binds within the insulator and that this site is important for generating in adjacent nucleosomes histone modifications associated with active chromatin and, by inference, with barrier function. To understand the mechanism of USF1 action, we have characterized USF1-containing complexes. USF1 interacts directly with the histone H4R3-specific methyltransferase PRMT1. USF1, PRMT1, and the histone acetyltransferases (HATs) PCAF and SRC-1 form a complex with both H4R3 histone methyltransferase and HAT activities. Small interfering RNA downregulation of USF1 results in localized loss of H4R3 methylation, and other histone modifications associated with euchromatin, at the insulator. A dominant negative peptide that interferes with USF1 binding to DNA causes silencing of an insulated reporter construct, indicating abolition of barrier function. These results show that USF1 plays a direct role in maintaining the barrier, supporting a model in which the insulator works as a barrier by maintaining a local environment of active chromatin.

AB - The insulator element at the 5′ end of the chicken β-globin locus acts as a barrier, protecting transgenes against silencing effects of adjacent heterochromatin. We showed earlier that the transcription factor USF1 binds within the insulator and that this site is important for generating in adjacent nucleosomes histone modifications associated with active chromatin and, by inference, with barrier function. To understand the mechanism of USF1 action, we have characterized USF1-containing complexes. USF1 interacts directly with the histone H4R3-specific methyltransferase PRMT1. USF1, PRMT1, and the histone acetyltransferases (HATs) PCAF and SRC-1 form a complex with both H4R3 histone methyltransferase and HAT activities. Small interfering RNA downregulation of USF1 results in localized loss of H4R3 methylation, and other histone modifications associated with euchromatin, at the insulator. A dominant negative peptide that interferes with USF1 binding to DNA causes silencing of an insulated reporter construct, indicating abolition of barrier function. These results show that USF1 plays a direct role in maintaining the barrier, supporting a model in which the insulator works as a barrier by maintaining a local environment of active chromatin.

UR - http://www.scopus.com/inward/record.url?scp=36048976921&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=36048976921&partnerID=8YFLogxK

U2 - 10.1128/MCB.01326-07

DO - 10.1128/MCB.01326-07

M3 - Article

C2 - 17846119

AN - SCOPUS:36048976921

VL - 27

SP - 7991

EP - 8002

JO - Molecular and Cellular Biology

JF - Molecular and Cellular Biology

SN - 0270-7306

IS - 22

ER -