PMID- 11461901
OWN - NLM
STAT- MEDLINE
DCOM- 20011101
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 276
IP  - 39
DP  - 2001 Sep 28
TI  - Maf and Jun nuclear oncoproteins share downstream target genes for inducing cell 
      transformation.
PG  - 36849-56
AB  - The Maf oncoprotein is a basic leucine zipper (bZip)-bearing transcriptional 
      activator that recognizes the Maf recognition element (MARE) DNA sequence. In 
      this study, we investigated the role of Maf's transactivation function in cell 
      transformation. Replacement of the conserved amino terminus transactivator domain 
      of Maf by a heterologous and stronger transactivator domain (the acidic 
      transactivator domain of VP16) resulted in enhanced transformation of chicken 
      embryo fibroblast cells. In contrast, the fusing of a transcriptional repressor 
      domain (Sin3 interaction domain of Mxi1) with the whole Maf protein masked the 
      transactivator function of Maf, which in turn inhibited its transforming 
      activity. Furthermore, the leucine zipper domain of Maf, which defines its 
      dimer-forming specificity, was exchangeable with that of GCN4 yeast protein in 
      terms of its transactivating and cell transforming activities. Thus, heterodimer 
      formation with other bZip factors is not required for Maf's ability to transform. 
      These results together suggest that transactivation through MARE is necessary for 
      Maf-induced transformation and that there exist downstream target gene(s) for 
      transformation. Since the MARE sequence overlaps with the recognition element of 
      another bZip oncoprotein Jun, we assessed whether Jun and Maf induce cell 
      transformation through activating the same genes. We thus constructed a mutated 
      version of Jun that has a GCN4 leucine zipper and lacks the transactivator 
      domain. This mutant repressed the cell transformation not only by Jun but also by 
      Maf. Thus, Maf and Jun share downstream target gene(s) that are involved in cell 
      transformation.
FAU - Kataoka, K
AU  - Kataoka K
AD  - Department of Virology, Institute of Medical Science, University of Tokyo, 4-6-1 
      Shirokanedai, Minato-ku, Tokyo 108-8639, Japan. kkataoka@bio.titech.ac.jp
FAU - Shioda, S
AU  - Shioda S
FAU - Yoshitomo-Nakagawa, K
AU  - Yoshitomo-Nakagawa K
FAU - Handa, H
AU  - Handa H
FAU - Nishizawa, M
AU  - Nishizawa M
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20010718
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Oncogene Protein p65(gag-jun))
RN  - 0 (Oncogene Protein v-maf)
RN  - 0 (Oncogene Proteins, Viral)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Viral Proteins)
RN  - 9007-49-2 (DNA)
RN  - EC 1.13.12.- (Luciferases)
SB  - IM
MH  - Animals
MH  - Base Sequence
MH  - Blotting, Western
MH  - Cell Nucleus/*enzymology/*metabolism
MH  - *Cell Transformation, Neoplastic
MH  - Chick Embryo
MH  - DNA/metabolism
MH  - DNA-Binding Proteins/*metabolism
MH  - Dimerization
MH  - Fibroblasts
MH  - Gene Deletion
MH  - Genes, Dominant
MH  - Humans
MH  - Leucine Zippers
MH  - Luciferases/metabolism
MH  - Molecular Sequence Data
MH  - Oncogene Protein p65(gag-jun)/*metabolism
MH  - Oncogene Protein v-maf
MH  - Oncogene Proteins, Viral/*metabolism
MH  - Phenotype
MH  - Plasmids/metabolism
MH  - Point Mutation
MH  - Protein Binding
MH  - Protein Structure, Tertiary
MH  - Rabbits
MH  - Recombinant Fusion Proteins/metabolism
MH  - Time Factors
MH  - Transcriptional Activation
MH  - *Viral Proteins
EDAT- 2001/07/20 10:00
MHDA- 2001/11/03 10:01
CRDT- 2001/07/20 10:00
PHST- 2001/07/20 10:00 [pubmed]
PHST- 2001/11/03 10:01 [medline]
PHST- 2001/07/20 10:00 [entrez]
AID - S0021-9258(20)86772-6 [pii]
AID - 10.1074/jbc.M102234200 [doi]
PST - ppublish
SO  - J Biol Chem. 2001 Sep 28;276(39):36849-56. doi: 10.1074/jbc.M102234200. Epub 2001 
      Jul 18.