An Exposed KID-Like Domain in Human T-Cell Lymphotropic Virus Type 1 Tax Is Responsible for the Recruitment of Coactivators CBP/p300

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Molecular and Cellular Biology, September 1998, p. 5052-5061, Vol. 18, No. 9
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

An Exposed KID-Like Domain in Human T-Cell Lymphotropic Virus Type 1 Tax Is Responsible for the Recruitment of Coactivators CBP/p300

Robert Harrod,¹ Yong Tang,¹ Christophe Nicot,¹ Hsieng S. Lu,² Alex Vassilev,³ Yoshihiro Nakatani,³ and Chou-Zen Giam¹^,^*

Department of Microbiology and Immunology, Uniformed Services University of the Health Sciences, Bethesda, Maryland 20814¹; Department of Protein Structure, Amgen Inc., Thousand Oaks, California 91320²; and Laboratory of Molecular Growth Regulation, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892-2753³

Received 7 April 1998/Returned for modification 18 May 1998/Accepted 9 June 1998

Human T-cell lymphotropic virus type 1 (HTLV-1) transcriptional activation is mediated by the viral transactivator, Tax, andthree 21-bp repeats (Tax response element [TxRE]) located in theU3 region of the viral long terminal repeat (LTR). Each TxRE containsa core cyclic AMP response element (CRE) flanked by 5' G-richand 3' C-rich sequences. The TxRE binds CREB (CRE-binding protein)and Tax to form a ternary complex and confers Tax-dependent transactivation.Recent data indicate that Tax functions as a specific link toconnect CREB-binding protein (CBP)/p300 in a phosphorylation-independentmanner to CREB/ATF-1 assembled on the viral 21-bp repeats. GlutathioneS-transferase pull-down performed with Tax deletion mutants andpeptide competition have localized the site in Tax critical forbinding CBP/p300 to a highly protease-sensitive region aroundamino acid residues 81 to 95 (₈₁QRTSKTLKVLTPPIT₉₅) which liesbetween the domains previously proposed to be important for CREBbinding and Tax subunit dimerization. Amino acid residues aroundthe trypsin- and chymotrypsin-sensitive sites (₈₈KVL₉₀) of Taxbear resemblance to those in the kinase-inducible domain of CREB(₁₂₉SRRPSYRKILNE₁₄₀) surrounding Ser-133, which undergoes signal-inducedphosphorylation to recruit CBP/p300. Site-directed mutagenesisof residues in this domain (R82A, K85A, K88A, and V89A) resultedin proteins which failed to transactivate from the HTLV-1 LTRin vivo. These mutants (K85A, K88A, and V89A) bind CREB with similaraffinities as wild-type Tax, yet interaction with CBP/p300 isabrogated in various biochemical assays, indicating that the recruitmentof CBP/p300 is crucial for Tax transactivation. A Tax mutant,M47, defective in the COOH-terminal transactivation domain, continuedto interact with CBP/p300, suggesting that interactions with additionalcellular factors are required for proper Tax function.

^* Corresponding author. Mailing address: Department of Microbiology and Immunology, Uniformed Services University of the HealthSciences, 4301 Jones Bridge Rd., Bethesda, MD 20814. Phone: (301)295-9624. Fax: (301) 295-1545. E-mail: giam{at}bob.usuf2.usuhs.mil.

Molecular and Cellular Biology, September 1998, p. 5052-5061, Vol. 18, No. 9
0270-7306/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

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