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Nucleic Acids Research, 1995, Vol. 23, No. 1 1-9
© 1995


MOLECULAR BIOLOGY

The c-myc protein represses the {lambda}5 and TdT initiators

Sabine Mai and Inga-Lill Mårtensson*

Basel Institute for Immunology Grenzacherstrasse 487, CH-4005 Basel, Switzerland

*To whom correspondence should be addressed

Received November 17, 1994. Accepted December 2, 1994.

The {lambda}5 promoter initiates transcription at multiple sites and confers expression in all cell types. Two {lambda}5 promoter–derived oligonucleotides (lnr{lambda}5:2 and lnr{lambda}5:1), each with a transcription start site, could promote transcription in transient transfection assays. In contrast, a third oligonucleotide (+90{lambda}5), without a transcription initiation site, was inactive. The lnr{lambda}5:1 and lnr{lambda}5:2 oligonucleotides formed a major DNA–protein complex B' in gel retardation analyses; no protein-DNA complexes were observed with the inactive +90 oligonucleotide. The B' complexes of lnr:{lambda}5:1 and lnr{lambda}5:2 each contained c-myc and myn (murine homologue of Max) proteins. The c-myc and myn proteins were also found to bind the TdT initiator (lnrTdT). Using mutated oligonucleotides, we found that the c-myc/myn proteins bound to the transcription initiation site of both lnr{lambda}5:1 and lnrTdT, however, these mutated oligonucleotides were inactive in transfection assays. This suggested that, in this system, transcription depended both on a transcription initiation site and appropriate flanking sequences. The significance of c-myc binding to the respective initiator was analysed by overexpressing c-myc in co-transfection assays. Under these conditions the transcriptional activity of both the {lambda}5 and the TdT initiator was repressed.


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