Dec 26, 2001

The conserved Mynd domain of BS69 binds cellular and oncoviral proteins through a common PXLXP motif

The Journal of Biological Chemistry
Stephane Ansieau, Achim Leutz

Abstract

BS69 is a transcriptional co-repressor protein and a potential tumor suppressor that binds to the adenoviral oncoprotein E1A. We show that the C-terminal Mynd domain of BS69 (amino acids 516-561) or the closely related Mynd domains of the Caenorhabditis elegans proteins Bra-1 and Bra-2 bind not only to E1A but also to the Epstein-Barr virus EBNA2 oncoprotein and the Myc-related cellular protein MGA. Interaction depends on intact PXLXP motifs present in all three proteins. Moreover, viral proteins compete for binding of BS69 to MGA in a PXLXP-dependent fashion. Because deletions in E1A or EBNA2 that cover the PXLXP motifs are non-transforming, our observations suggest a role for BS69 in cell growth control that is reminiscent of abrogation of the Rb function by various oncoproteins.

Mentioned in this Paper

Mga protein, mouse
ZMYND11 gene
Conserved Sequence
Precipitin Tests
Tumor Suppressor Genes
Transfection
Transcription Repressor/Corepressor
Carboxy-Terminal Amino Acid
Chimeric Proteins, Recombinant
Caenorhabditis elegans

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