CG&D
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Cancer Research Clinical Cancer Research
Cancer Epidemiology Biomarkers & Prevention Molecular Cancer Therapeutics
Molecular Cancer Research Cell Growth & Differentiation

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Furukawa, K.
Right arrow Articles by Ito, Y.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Furukawa, K.
Right arrow Articles by Ito, Y.

Cell Growth & Differentiation, Vol 1, Issue 3 135-147, Copyright © 1990 by American Association of Cancer Research


ARTICLES

A ubiquitous repressor interacting with an F9 cell-specific silencer and its functional suppression by differentiated cell-specific positive factors

K Furukawa, Y Yamaguchi, E Ogawa, K Shigesada, M Satake and Y Ito
Departments of Viral Oncology, Kyoto University, Japan.

A mutant of polyomavirus, F9-5000, capable of growing in F9 cell [M. Vasseur et al., J. Virol., 43: 800-808, 1982 (1)], has a deletion in the enhancer from nucleotide 5119 to nucleotide 5142. The oligonucleotide corresponding to the deleted region (delta F9-5000 element) showed silencer activity on gene expression in F9 cells. Mobility shift assay revealed a nuclear factor, PEBP4, in F9 nuclear extract which bound to the delta F9-5000 element. Mutations introduced into the PEBP4 binding site specifically abolished its binding as well as the inhibitory effect on gene expression. After F9 cells were induced to differentiate, two more factors, PEBP2 and PEBP1, a member of AP1 family, became detectable in addition to PEBP4, and at the same time the delta F9-5000 element lost silencer activity and acquired an enhancer activity. The recognition sequence of PEBP2 as well as that of PEBP1 overlapped with that of a repressor, PEBP4. PEBP4 and PEBP3, a factor related to PEBP2, were shown to compete for binding to delta F9-5000. Interplay of a ubiquitous negative factor and differentiation-induced positive factors may represent one aspect of the gene regulation during embryonic development.


This article has been cited by other articles:


Home page
J Biol ChemHome page
Y. Yamaguchi, M. Kurokawa, Y. Imai, K. Izutsu, T. Asai, M. Ichikawa, G. Yamamoto, E. Nitta, T. Yamagata, K. Sasaki, et al.
AML1 Is Functionally Regulated through p300-mediated Acetylation on Specific Lysine Residues
J. Biol. Chem., April 9, 2004; 279(15): 15630 - 15638.
[Abstract] [Full Text] [PDF]


Home page
Microbiol. Mol. Biol. Rev.Home page
K. A. Gottlieb and L. P. Villarreal
Natural Biology of Polyomavirus Middle T Antigen
Microbiol. Mol. Biol. Rev., June 1, 2001; 65(2): 288 - 318.
[Abstract] [Full Text] [PDF]


Home page
BloodHome page
Y. Imai, M. Kurokawa, K. Izutsu, A. Hangaishi, K. Takeuchi, K. Maki, S. Ogawa, S. Chiba, K. Mitani, and H. Hirai
Mutations of the AML1 gene in myelodysplastic syndrome and their functional implications in leukemogenesis
Blood, November 1, 2000; 96(9): 3154 - 3160.
[Abstract] [Full Text] [PDF]


Home page
J Biol ChemHome page
X.-F. Le, Y. Groner, S. M. Kornblau, Y. Gu, W. N. Hittelman, D. Levanon, K. Mehta, R. B. Arlinghaus, and K.-S. Chang
Regulation of AML2/CBFA3 in Hematopoietic Cells through the Retinoic Acid Receptor {alpha}-Dependent Signaling Pathway
J. Biol. Chem., July 30, 1999; 274(31): 21651 - 21658.
[Abstract] [Full Text] [PDF]


Home page
J. Immunol.Home page
M.-J. Shi and J. Stavnezer
CBF{alpha}3 (AML2) Is Induced by TGF-{beta}1 to Bind and Activate the Mouse Germline Ig {alpha} Promoter
J. Immunol., December 15, 1998; 161(12): 6751 - 6760.
[Abstract] [Full Text] [PDF]


Home page
J Biol ChemHome page
M. Kurokawa, T. Tanaka, K. Tanaka, N. Hirano, S. Ogawa, K. Mitani, Y. Yazaki, and H. Hirai
A Conserved Cysteine Residue in the runt Homology Domain of AML1 Is Required for the DNA Binding Ability and the Transforming Activity on Fibroblasts
J. Biol. Chem., July 12, 1996; 271(28): 16870 - 16876.
[Abstract] [Full Text] [PDF]


Home page
J Biol ChemHome page
V. Geoffroy, P. Ducy, and G. Karsenty
A PEBP2/AML-1-related Factor Increases Osteocalcin Promoter Activity through Its Binding to an Osteoblast-specific cis-Acting Element
J. Biol. Chem., December 29, 1995; 270(52): 30973 - 30979.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Cancer Research Clinical Cancer Research
Cancer Epidemiology Biomarkers & Prevention Molecular Cancer Therapeutics
Molecular Cancer Research Cell Growth & Differentiation
Copyright © 1990 by the American Association of Cancer Research.