Scaffold/matrix attachment region elements interact with a p300-scaffold attachment factor A complex and are bound by acetylated nucleosomes

J. H A Martens, Matty Verlaan, Eric Kalkhoven, Josephine C. Dorsman, Alt Zantema*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

80 Citations (Scopus)

Abstract

The transcriptional coactivator p300 regulates transcription by binding to proteins involved in transcription and by acetylating histones and other proteins. These transcriptional effects are mainly at promoter and enhancer elements. Regulation of transcription also occurs through scaffold/matrix attachment regions (S/MARs), the chromatin regions that bind the nuclear matrix. Here we show that p300 binds to the S/MAR binding protein scaffold attachment factor A (SAF-A), a major constituent of the nuclear matrix. Using chromatin immunoprecipitations, we established that both p300 and SAF-A bind to S/MAR elements in the transiently silent topoisomerase I gene prior to its activation at G1 during cell cycle. This binding is accompanied by local acetylation of nucleosomes, suggesting that p300-SAF-A interactions at S/MAR elements of nontranscribed genes might poise these genes for transcription.

Original languageEnglish
Pages (from-to)2598-2606
Number of pages9
JournalMolecular and Cellular Biology
Volume22
Issue number8
DOIs
Publication statusPublished - 10 Apr 2002

Fingerprint

Dive into the research topics of 'Scaffold/matrix attachment region elements interact with a p300-scaffold attachment factor A complex and are bound by acetylated nucleosomes'. Together they form a unique fingerprint.

Cite this