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Nucleic Acids Research, 1993, Vol. 21, No. 3 523-529
© 1993

MOLECULAR BIOLOGY

Oncogenic conversion of Ets affects redox regulation in-vivo and in-vitro

Christine Wasylyk and Bohdan Wasylyk*

CNRS-LGME/INSERM-U. 184, Instftut de Chimie Biologique, Faculté de Médecine 11 rue Humann, 67085 Strasbourg Cedex, France

*To whom correspondence should be addressed

Received October 20, 1992. Revised December 21, 1992. Accepted December 21, 1992.

The avian acute leukemia virus E26 encodes a fusion protein between viral Gag and the cellular transcription factors cMyb and cEtsl(p68). vEts on its own transforms more mature erythroid cells. We have compared the properties of vEts and cEtsl(p68). vEts interacts preferentially with an antibody that recognizes the active conformation of the DNA-binding domain. The DNA-binding, activity of vEts is particularly sensitive to incubation conditions for band-shift assays, phosphorylation and modification by sulphydryl specific reagents. increased sensitivity is due to loss of a protective function of cEtsi C-terminal sequences. cEts2 has a related C-terminal sequence with a similar role. These results suggest that the vEts DNA-binding domain is more accessible to protein-protein interactions and to regulatory mechanisms. Indeed, vEts DNA binding is preferentially inactivated by oxidizing conditions in-vivo. We suggest that the ‘open’ conformation of the vEts DNA-binding domain favours interactions with other proteins or DNA and facilitates transformation.


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