Nucleic Acids Research, 1994, Vol. 22, No. 7 1305-1312
© 1994
MOLECULAR BIOLOGY |
Activation of c-Jun transcription factor by substitution of a charged residue in its N-terminal domain
Department of Dermatology, Stanford University Medical School Stanford, CA 94305 1Department of Cell Genetics, Genentech Inc. 460 Point San Bruno Boulevard, South San Francisco, CA 94080, USA
*To whom correspondence should be addressed
Received March 29, 1993. Revised March 2, 1994. Accepted March 2, 1994.
C-Jun is a cellular transcription factor that can control gene expression in response to treatment of cells with phorbol esters, growth factors, and expression of some oncogenes. The ability of c-Jun to catalyze the transcription of certain genes is controlled, in part, by changes in the phosphorylatlon state of specific amlno acids in c-Jun. One of the major sites that is phosphorylated during signal response is Ser73. Here we show that substitution of a negatively charged aspartic acid residue at 73 constitutlvely increased transcriptional activity of c-Jun. The Asp73 substitution also enhanced its avalllblllty to bind to DNA in a whole cell extract without altering its intrinsic DNA binding activity since the intrinsic activity was unaltered for the c-Jun mutant proteins expressed in a bacterial system. The negatively charged Asp substitution may mimic the negative charge of a phosphorylated serlne at 73. The substitution of an uncharged alanine at 73 resulted in lowered activities. The N-terminal end of c-Jun containing these substitutions was fused to the DNA-bindlng region of the bovine papilloma virus E2 protein, and was able to confer the same activation properties to the fusion protein at the heterologous E2 DNA-binding site. Ser73 lies in a region of c-Jun previously proposed to bind an uncharacterlzed inhibitor, perhaps related to a protein of approximately 17.5 kD that copreclpltates along with our c-Jun or the JunE2 fusion products.
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