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Journal of Virology, February 2002, p. 1461-1474, Vol. 76, No. 3
0022-538X/01/$04.00+0     DOI: 10.1128/JVI.76.3.1461-1474.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Adenovirus E1A N-Terminal Amino Acid Sequence Requirements for Repression of Transcription In Vitro and In Vivo Correlate with Those Required for E1A Interference with TBP-TATA Complex Formation

Janice M. Boyd, Paul M. Loewenstein, Qing-quan Tang, Li Yu,,{dagger} and Maurice Green*

Institute for Molecular Virology, Saint Louis University School of Medicine, St. Louis, Missouri 63110

Received 16 August 2001/ Accepted 17 October 2001

The adenovirus (Ad) E1A 243R oncoprotein encodes an N-terminal transcription repression domain that is essential for early viral functions, cell immortalization, and cell transformation. The transcription repression function requires sequences within amino acids 1 to 30 and 48 to 60. To elucidate the roles of the TATA-binding protein (TBP), p300, and the CREB-binding protein (CBP) in the mechanism(s) of E1A repression, we have constructed 29 amino acid substitution mutants and 5 deletion mutants spanning the first 30 amino acids within the E1A 1-80 polypeptide backbone. These mutant E1A polypeptides were characterized with regard to six parameters: the ability to repress transcription in vitro and in vivo, to disrupt TBP-TATA box interaction, and to bind TBP, p300, and CBP. Two regions within E1A residues 1 to 30, amino acids 2 to 6 and amino acid 20, are critical for E1A transcription repression in vitro and in vivo and for the ability to interfere with TBP-TATA interaction. Replacement of 6Cys with Ala in the first region yields the most defective mutant. Replacement of 20Leu with Ala, but not substitutions in flanking residues, yields a substantially defective phenotype. Protein binding assays demonstrate that replacement of 6Cys with Ala yields a mutant completely defective in interaction with TBP, p300, and CBP. Our findings are consistent with a model in which the E1A repression function involves interaction of E1A with p300/CBP and interference with the formation of a TBP-TATA box complex.

* Corresponding author. Mailing address: Institute for Molecular Virology, Saint Louis University School of Medicine, St. Louis, MO 63110. Phone: (314) 577-8401. Fax: (314) 577-8406. E-mail: green{at}slu.edu.

{dagger} Present address: Center for Biologics Evaluation and Research, Food and Drug Administration, Bethesda, Md.

Journal of Virology, February 2002, p. 1461-1474, Vol. 76, No. 3
0022-538X/01/$04.00+0     DOI: 10.1128/JVI.76.3.1461-1474.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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