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

Item Type:Article
Title:The conserved Mynd domain of BS69 binds cellular and oncoviral proteins through a common PXLXP motif
Creators Name:Ansieau, S. and Leutz, A.
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.
Keywords:Adenoviridae, Adenovirus E1A Proteins, Amino Acid Motifs, Amino Acid Sequence, Amino Acid Sequence Homology, Caenorhabditis Elegans, Carrier Proteins, Competitive Binding, Complementary DNA, Conserved Sequence, Epstein-Barr Virus Nuclear Antigens, Gene Deletion, Genetic Transcription, Glutathione Transferase, Hela Cells, Molecular Sequence Data, Peptides, Plasmids, Precipitin Tests, Protein Binding, Tertiary Protein Structure, Trans-Activation, Transcription Factors, Transfection, Two-Hybrid System Techniques, Viral Proteins, Animals
Source:Journal of Biological Chemistry
ISSN:0021-9258
Publisher:American Society for Biochemistry and Molecular Biology (U.S.A.)
Volume:277
Number:7
Page Range:4906-4910
Date:1 January 2002
PubMed:View item in PubMed

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