Binding of the c-myb proto-oncogene product to the simian virus 40 enhancer stimulates transcription

The proto-oncogene c-myb encodes a nuclear protein which binds to DNA. Here we find that bacterially synthesized c-myb protein binds to one site of the simian virus 40 enhancer. The c-myb protein purified from the human T-cell line, Molt4, was also shown to recognize the same sequence. In co-transfe...

Full description

Saved in:
Bibliographic Details
Published in:The Journal of biological chemistry 1990-02, Vol.265 (6), p.3479-3483
Main Authors: Nakagoshi, H, Nagase, T, Kanei-Ishii, C, Ueno, Y, Ishii, S
Format: Article
Language:English
Subjects:
Animals
Base Sequence
Biological and medical sciences
Cell Line
Enhancer Elements, Genetic
Fundamental and applied biological sciences. Psychology
Humans
Mice
Molecular and cellular biology
Molecular genetics
Molecular Sequence Data
Nuclear Proteins - metabolism
Plasmids
Protein-Tyrosine Kinases - metabolism
Proto-Oncogene Proteins - isolation & purification
Proto-Oncogene Proteins - metabolism
Proto-Oncogene Proteins c-myb
Proto-Oncogenes
Recombinant Proteins - isolation & purification
Recombinant Proteins - metabolism
Simian virus 40 - genetics
Transcription, Genetic
Transcription. Transcription factor. Splicing. Rna processing
Transfection
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The proto-oncogene c-myb encodes a nuclear protein which binds to DNA. Here we find that bacterially synthesized c-myb protein binds to one site of the simian virus 40 enhancer. The c-myb protein purified from the human T-cell line, Molt4, was also shown to recognize the same sequence. In co-transfection experiments with a c-myb expression plasmid, tandem repeats of a c-myb-binding sequence were shown to function as a c-myb-dependent enhancer. These results indicate the c-myb protein is a simian virus 40 enhancer-binding protein that can positively regulate transcription.
ISSN:0021-9258
1083-351X
DOI:10.1016/S0021-9258(19)39793-5