PMID- 9565602
OWN - NLM
STAT- MEDLINE
DCOM- 19980605
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 273
IP  - 19
DP  - 1998 May 8
TI  - Multivalent DNA binding complex generated by small Maf and Bach1 as a possible 
      biochemical basis for beta-globin locus control region complex.
PG  - 11783-90
AB  - The human beta-globin locus control region (LCR) is required to properly regulate 
      chromatin domain opening, replication timing, and globin gene activation. The LCR 
      contains multiple NF-E2 sites (Maf recognition elements, MAREs) that allow the 
      binding of various basic leucine zipper (bZip) proteins like p45 NF-E2, Nrf1, 
      Nrf2, Bach1, and Bach2, in some cases as obligate heterodimers with a small Maf 
      protein. In addition to the bZip domain, the Bach proteins bear a BTB/POZ domain, 
      which has been implicated in the regulation of chromatin structure. We show here 
      that Bach1 is highly expressed in hematopoietic cells and constitutes one of the 
      two MARE-binding activities in murine erythroleukemic (MEL) cells. We further 
      demonstrate that Bach1/MafK heterodimers interact with each other through the BTB 
      domain, generating a multimeric and multivalent DNA binding complex. These 
      results strongly implicate Bach1/MafK heterodimer as an architectural 
      transcription factor that mediates interactions among multiple MAREs. Such a 
      factor could then provide a model for assembly of the theoretical beta-globin LCR 
      "holocomplex. " Other BTB domain proteins have already been demonstrated to be 
      involved in remodeling chromatin, and thus this class of proteins likely promote 
      the formation of nucleoprotein complexes required to establish the architecture 
      of regulatory domains.
FAU - Igarashi, K
AU  - Igarashi K
AD  - Institute of Basic Medical Sciences and Center for Tsukuba Advanced Research 
      Alliance, University of Tsukuba, Tenno-dai 1-1-1, Tsukuba 305, Japan.
FAU - Hoshino, H
AU  - Hoshino H
FAU - Muto, A
AU  - Muto A
FAU - Suwabe, N
AU  - Suwabe N
FAU - Nishikawa, S
AU  - Nishikawa S
FAU - Nakauchi, H
AU  - Nakauchi H
FAU - Yamamoto, M
AU  - Yamamoto M
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (BACH1 protein, human)
RN  - 0 (Bach1 protein, mouse)
RN  - 0 (Basic-Leucine Zipper Transcription Factors)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Erythroid-Specific DNA-Binding Factors)
RN  - 0 (Fanconi Anemia Complementation Group Proteins)
RN  - 0 (MAFK protein, human)
RN  - 0 (MafK Transcription Factor)
RN  - 0 (Mafk protein, mouse)
RN  - 0 (NF-E2 Transcription Factor)
RN  - 0 (NF-E2 Transcription Factor, p45 Subunit)
RN  - 0 (NFE2 protein, human)
RN  - 0 (Nfe2 protein, mouse)
RN  - 0 (Nuclear Proteins)
RN  - 0 (Transcription Factors)
RN  - 9004-22-2 (Globins)
SB  - IM
MH  - Animals
MH  - Basic-Leucine Zipper Transcription Factors
MH  - Binding Sites
MH  - Bone Marrow Cells
MH  - DNA-Binding Proteins/*metabolism
MH  - Dimerization
MH  - Erythroid-Specific DNA-Binding Factors
MH  - Fanconi Anemia Complementation Group Proteins
MH  - Female
MH  - Gene Expression Regulation
MH  - Globins/*genetics
MH  - *Hematopoiesis
MH  - Humans
MH  - MafK Transcription Factor
MH  - Mice
MH  - Mice, Inbred C57BL
MH  - NF-E2 Transcription Factor
MH  - NF-E2 Transcription Factor, p45 Subunit
MH  - Nuclear Proteins/*physiology
MH  - Protein Binding
MH  - Transcription Factors/*metabolism/*physiology
MH  - Transcriptional Activation
EDAT- 1998/06/13 00:00
MHDA- 1998/06/13 00:01
CRDT- 1998/06/13 00:00
PHST- 1998/06/13 00:00 [pubmed]
PHST- 1998/06/13 00:01 [medline]
PHST- 1998/06/13 00:00 [entrez]
AID - S0021-9258(19)89388-2 [pii]
AID - 10.1074/jbc.273.19.11783 [doi]
PST - ppublish
SO  - J Biol Chem. 1998 May 8;273(19):11783-90. doi: 10.1074/jbc.273.19.11783.