PMID- 10428834 OWN - NLM STAT- MEDLINE DCOM- 19990902 LR - 20210209 IS - 0021-9258 (Print) IS - 0021-9258 (Linking) VI - 274 IP - 32 DP - 1999 Aug 6 TI - Retinoid-dependent recruitment of a histone H1 displacement activity by retinoic acid receptor. PG - 22563-8 AB - Targeted recruitment of histone acetyltransferase (HAT) activities by sequence-specific transcription factors, including the retinoic acid receptors (RARs) and retinoid X receptors (RXRs), has been proposed to lead to destabilization of nucleosomal cores by acetylation of core histones. However, biochemical evidence indicates that destabilization and depletion of linker H1 histones must also occur at the promoter regions of actively transcribing genes. Mechanisms by which nuclear receptors and other transcription factors affect the removal of histone H1 from transcriptionally silent chromatin have not been previously described. In this report, we show that RARs interact in a ligand-dependent manner with HMG-I, which is known to displace histone H1 from chromatin. We further show that HMG-I and a novel related protein, HMG-R, also interact with other transcription factors. Using sense and antisense constructs of HMG-I/R in transient transfection assays with a retinoid responsive reporter, we also demonstrate that HMG-I/R is important for retinoid dependent transcriptional activity of RAR. These findings suggest a step wise mechanism by which RARs and other transcription factors can cause a targeted unfolding of compact chromatin as a first step in transcriptional activation, which would then be followed by recruitment of HAT activity and subsequent events. FAU - Nagpal, S AU - Nagpal S AD - Retinoid Research, Allergan Inc., Irvine, California 92713, USA. nagpal_sunil@allergan.com FAU - Ghosn, C AU - Ghosn C FAU - DiSepio, D AU - DiSepio D FAU - Molina, Y AU - Molina Y FAU - Sutter, M AU - Sutter M FAU - Klein, E S AU - Klein ES FAU - Chandraratna, R A AU - Chandraratna RA LA - eng PT - Journal Article PL - United States TA - J Biol Chem JT - The Journal of biological chemistry JID - 2985121R RN - 0 (Chromatin) RN - 0 (High Mobility Group Proteins) RN - 0 (Histones) RN - 0 (Ligands) RN - 0 (Nuclear Proteins) RN - 0 (Proto-Oncogene Proteins c-jun) RN - 0 (Receptors, Cytoplasmic and Nuclear) RN - 0 (Receptors, Retinoic Acid) RN - 0 (Retinoid X Receptors) RN - 0 (Retinoids) RN - 0 (Saccharomyces cerevisiae Proteins) RN - 0 (Trans-Activators) RN - 0 (Transcription Factors) RN - EC 2.3.1.- (Acetyltransferases) RN - EC 2.3.1.48 (CREB-Binding Protein) RN - EC 2.3.1.48 (CREBBP protein, human) RN - EC 2.3.1.48 (Histone Acetyltransferases) SB - IM MH - Acetylation MH - Acetyltransferases/metabolism MH - Amino Acid Sequence MH - CREB-Binding Protein MH - Chromatin/metabolism MH - High Mobility Group Proteins/*metabolism MH - Histone Acetyltransferases MH - Histones/*metabolism MH - Humans MH - Ligands MH - Molecular Sequence Data MH - Nuclear Proteins/metabolism MH - Protein Binding MH - Proto-Oncogene Proteins c-jun/metabolism MH - Receptors, Cytoplasmic and Nuclear/metabolism MH - Receptors, Retinoic Acid/*metabolism MH - Retinoid X Receptors MH - Retinoids/*metabolism MH - *Saccharomyces cerevisiae Proteins MH - Trans-Activators/metabolism MH - Transcription Factors/metabolism MH - *Transcriptional Activation EDAT- 1999/07/31 00:00 MHDA- 1999/07/31 00:01 CRDT- 1999/07/31 00:00 PHST- 1999/07/31 00:00 [pubmed] PHST- 1999/07/31 00:01 [medline] PHST- 1999/07/31 00:00 [entrez] AID - S0021-9258(18)81577-0 [pii] AID - 10.1074/jbc.274.32.22563 [doi] PST - ppublish SO - J Biol Chem. 1999 Aug 6;274(32):22563-8. doi: 10.1074/jbc.274.32.22563.