PMID- 9614938
OWN - NLM
STAT- MEDLINE
DCOM- 19980625
LR  - 20081121
IS  - 0022-2836 (Print)
IS  - 0022-2836 (Linking)
VI  - 278
IP  - 4
DP  - 1998 May 15
TI  - The mouse mammary tumour virus promoter positioned on a tetramer of histones H3 
      and H4 binds nuclear factor 1 and OTF1.
PG  - 725-39
AB  - Modulation of eukaryotic gene expression is influenced by the organization of 
      regulatory DNA-elements in chromatin. The mouse mammary tumor virus (MMTV) 
      promoter exhibits regularly positioned nucleosomes that reduce the accessibility 
      of the binding sites for sequence-specific transcription factors, in particular 
      nuclear factor (NF1). Hormonal induction of the MMTV promoter is accompanied by 
      remodeling of the nucleosomal structure, but the biochemical nature of these 
      structural changes is unknown. Using recombinant histones, we have now assembled 
      the MMTV promoter in particles containing either an octamer of the histones H3, 
      H4, H2A and H2B or a tetramer of histones H3 and H4, and have compared the two 
      particles in terms of structure, positioning, and exclusion of transcription 
      factors. Using site-directed hydroxy radicals to map histone locations, two main 
      nucleosome positions are found with dyads at position -107 and at -127. The same 
      two main positions are found for particles containing only the H3/H4 tetramer, 
      showing that the absence of H2A/H2B dimers does not alter positioning. The 
      rotational orientation of the DNA double helix in both types of particles is 
      essentially identical. However, the ends of the nucleosomal DNA as well as its 
      central region are more accessible to cleavage reagents in the tetramer particle 
      than in the octamer particle. In agreement with these structural features, the 
      transcription factors NF1 and OTF1 were able to bind to their cognate sites on 
      the tetramer particle, while they could not gain access to the same sites on the 
      surface of the octamer particle. The DNase I digestion pattern of octamers 
      treated with partially purified SWI/SNF complex from HeLa cells in the presence 
      of ATP is indistinguishable from that of tetramer particles, suggesting that the 
      SWI/SNF complex promotes ATP-dependent remodeling of the octamer particle but not 
      of tetramer particles. These results are compatible with a hormone-induced 
      removal of histone H2A/H2B during MMTV induction.
FAU - Spangenberg, C
AU  - Spangenberg C
AD  - Institut fur Molekularbiologie und Tumorforshung, Philipps-Universitat, Marburg, 
      Germany.
FAU - Eisfeld, K
AU  - Eisfeld K
FAU - Stunkel, W
AU  - Stunkel W
FAU - Luger, K
AU  - Luger K
FAU - Flaus, A
AU  - Flaus A
FAU - Richmond, T J
AU  - Richmond TJ
FAU - Truss, M
AU  - Truss M
FAU - Beato, M
AU  - Beato M
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - Netherlands
TA  - J Mol Biol
JT  - Journal of molecular biology
JID - 2985088R
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (HCFC1 protein, human)
RN  - 0 (Histones)
RN  - 0 (Host Cell Factor C1)
RN  - 0 (NFI Transcription Factors)
RN  - 0 (Nucleosomes)
RN  - 0 (Octamer Transcription Factor-1)
RN  - 0 (POU2F1 protein, human)
RN  - 0 (Recombinant Proteins)
RN  - 0 (Transcription Factors)
RN  - 0 (transcription factor nuclear factor 1)
RN  - 3352-57-6 (Hydroxyl Radical)
RN  - EC 3.6.1.- (Adenosine Triphosphatases)
SB  - IM
MH  - Adenosine Triphosphatases/metabolism
MH  - DNA Footprinting
MH  - DNA-Binding Proteins/*metabolism
MH  - Gene Expression Regulation
MH  - HeLa Cells
MH  - Histones/genetics/*metabolism
MH  - Host Cell Factor C1
MH  - Humans
MH  - Hydroxyl Radical
MH  - Mammary Tumor Virus, Mouse/*genetics
MH  - Molecular Conformation
MH  - Molecular Structure
MH  - NFI Transcription Factors
MH  - Nucleosomes/*metabolism
MH  - Octamer Transcription Factor-1
MH  - *Promoter Regions, Genetic
MH  - Protein Binding
MH  - Recombinant Proteins/metabolism
MH  - Transcription Factors/*metabolism
MH  - Transcription, Genetic
EDAT- 1998/06/06 00:00
MHDA- 1998/06/06 00:01
CRDT- 1998/06/06 00:00
PHST- 1998/06/06 00:00 [pubmed]
PHST- 1998/06/06 00:01 [medline]
PHST- 1998/06/06 00:00 [entrez]
AID - S0022-2836(98)91718-1 [pii]
AID - 10.1006/jmbi.1998.1718 [doi]
PST - ppublish
SO  - J Mol Biol. 1998 May 15;278(4):725-39. doi: 10.1006/jmbi.1998.1718.