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Negative autoregulation of c-Myb activity by homodimer formation through the leucine zipper.

Authors
  • Nomura, T
  • Sakai, N
  • Sarai, A
  • Sudo, T
  • Kanei-Ishii, C
  • Ramsay, R G
  • Favier, D
  • Gonda, T J
  • Ishii, S
Type
Published Article
Journal
The Journal of biological chemistry
Publication Date
Oct 15, 1993
Volume
268
Issue
29
Pages
21914–21923
Identifiers
PMID: 8408047
Source
Medline
License
Unknown

Abstract

The trans-activating and transforming capacities of the c-myb proto-oncogene product (c-Myb) are negatively regulated through a leucine zipper structure in its negative regulatory domain. We show here tht in cotransfection assays, maximal Myb-induced trans-activation occurs with relatively low amounts of wild-type c-Myb, while higher levels of c-Myb result in reduced Myb-induced trans-activation. By contrast, this apparent negative autoregulation is not observed with a c-Myb mutant containing an impaired leucine zipper. Data presented here suggest that this negative autoregulation of trans-activation by wild-type c-Myb is a consequence of homodimer formation by c-Myb through its leucine zipper and of the inability of c-Myb dimers to bind DNA. These findings point to a novel mechanism of regulation of a transcription factor.

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