PMID- 10601024
OWN - NLM
STAT- MEDLINE
DCOM- 20000127
LR  - 20181130
IS  - 0261-4189 (Print)
IS  - 0261-4189 (Linking)
VI  - 18
IP  - 24
DP  - 1999 Dec 15
TI  - Mga, a dual-specificity transcription factor that interacts with Max and contains
      a T-domain DNA-binding motif.
PG  - 7019-28
AB  - The basic-helix-loop-helix-leucine zipper (bHLHZip) proteins Myc, Mad and Mnt are
      part of a transcription activation/repression system involved in the regulation
      of cell proliferation. The function of these proteins as transcription factors is
      mediated by heterodimerization with the small bHLHZip protein Max, which is
      required for their specific DNA binding to E-box sequences. We have identified a 
      novel Max-interacting protein, Mga, which contains a Myc-like bHLHZip motif, but 
      otherwise shows no relationship with Myc or other Max-interacting proteins. Like 
      Myc, Mad and Mnt proteins, Mga requires heterodimerization with Max for binding
      to the preferred Myc-Max-binding site CACGTG. In addition to the bHLHZip domain, 
      Mga contains a second DNA-binding domain: the T-box or T-domain. The T-domain is 
      a highly conserved DNA-binding motif originally defined in Brachyury and
      characteristic of the Tbx family of transcription factors. Mga binds the
      preferred Brachyury-binding sequence and represses transcription of reporter
      genes containing promoter-proximal Brachyury-binding sites. Surprisingly, Mga is 
      converted to a transcription activator of both Myc-Max and Brachyury
      site-containing reporters in a Max-dependent manner. Our results suggest that Mga
      functions as a dual-specificity transcription factor that regulates the
      expression of both Max-network and T-box family target genes.
FAU - Hurlin, P J
AU  - Hurlin PJ
AD  - Division of Basic Sciences, Fred Hutchinson Cancer Research Center, 1100 Fairview
      Avenue N., Seattle, WA 98109-1024, USA. pjh@shcc.org
FAU - Steingrimsson, E
AU  - Steingrimsson E
FAU - Copeland, N G
AU  - Copeland NG
FAU - Jenkins, N A
AU  - Jenkins NA
FAU - Eisenman, R N
AU  - Eisenman RN
LA  - eng
SI  - GENBANK/AF205935
GR  - CA20525/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - EMBO J
JT  - The EMBO journal
JID - 8208664
RN  - 0 (Basic Helix-Loop-Helix Leucine Zipper Transcription Factors)
RN  - 0 (Basic-Leucine Zipper Transcription Factors)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Fetal Proteins)
RN  - 0 (Mga protein, mouse)
RN  - 0 (Myc associated factor X)
RN  - 0 (Proto-Oncogene Proteins c-myc)
RN  - 0 (Recombinant Proteins)
RN  - 0 (T-Box Domain Proteins)
RN  - 0 (Transcription Factors)
RN  - 137468-70-3 (Max protein, mouse)
RN  - EQ43SC3GDB (Brachyury protein)
SB  - IM
EIN - EMBO J 2000 Jul 17;19(14):3841
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Basic Helix-Loop-Helix Leucine Zipper Transcription Factors
MH  - Basic-Leucine Zipper Transcription Factors
MH  - Binding Sites
MH  - Cloning, Molecular
MH  - DNA-Binding Proteins/*chemistry/*metabolism
MH  - Dimerization
MH  - Embryonic and Fetal Development
MH  - Fetal Proteins/genetics/metabolism
MH  - *Gene Expression Regulation, Developmental
MH  - Helix-Loop-Helix Motifs
MH  - Leucine Zippers
MH  - Mice
MH  - Molecular Sequence Data
MH  - Proto-Oncogene Proteins c-myc/chemistry/metabolism
MH  - Recombinant Proteins/chemistry/metabolism
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
MH  - T-Box Domain Proteins/genetics/metabolism
MH  - Transcription Factors/chemistry/*genetics/*metabolism
PMC - PMC1171765
EDAT- 1999/12/22 00:00
MHDA- 1999/12/22 00:01
CRDT- 1999/12/22 00:00
PHST- 1999/12/22 00:00 [pubmed]
PHST- 1999/12/22 00:01 [medline]
PHST- 1999/12/22 00:00 [entrez]
AID - 10.1093/emboj/18.24.7019 [doi]
PST - ppublish
SO  - EMBO J. 1999 Dec 15;18(24):7019-28. doi: 10.1093/emboj/18.24.7019.