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Molecular and Cellular Biology, July 2002, p. 5054-5063, Vol. 22, No. 14
0270-7306/02/$04.00+0     DOI: 10.1128/MCB.22.14.5054-5063.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

TRRAP-Dependent and TRRAP-Independent Transcriptional Activation by Myc Family Oncoproteins

Mikhail A. Nikiforov, Sanjay Chandriani, Jeonghyeon Park, Iulia Kotenko, Dina Matheos, Anna Johnsson, Steven B. McMahon, and Michael D. Cole*

Department of Molecular Biology, Princeton University, Princeton, New Jersey 08544-1014

Received 19 December 2001/ Returned for modification 8 February 2002/ Accepted 11 April 2002

We demonstrate that transformation-transactivation domain-associated protein (TRRAP) binding and the recruitment of histone H3 and H4 acetyltransferase activities are required for the transactivation of a silent telomerase reverse transcriptase (TERT) gene in exponentially growing human fibroblasts by c-Myc or N-Myc protein. However, recruitment of TRRAP by c- or N-Myc is dispensable for the partial induction of several basally expressed genes in exponentially growing primary and immortalized fibroblasts. Furthermore, recruitment of TRRAP is required for c-Myc- or N-Myc-mediated oncogenic transformation but not for the partial restoration of the growth defect in myc-null fibroblasts. A segment of the adenovirus E1A protein fused to a transformation-defective N-Myc protein carrying a small deletion in the transactivation domain specifically restores interaction with TRRAP, activates the silent TERT gene, induces acetylation of histones H3 and H4 at the TERT promoter, and transforms primary cells. Accordingly, wild-type L-Myc is much less efficient in TRRAP binding, activation of the silent TERT gene, and transformation of primary fibroblasts. Nevertheless, L-Myc is a potent activator of several basally expressed genes and can fully restore the growth defect of myc-null cells. These results suggest a differential requirement for TRRAP for several Myc-mediated activities.

* Corresponding author. Mailing address: Department of Molecular Biology, Princeton University, Washington Rd., Princeton, NJ 08544-1014. Phone: (609) 258-5936. Fax: (609) 258-4575. E-mail: mcole{at}molbio.princeton.edu.

Molecular and Cellular Biology, July 2002, p. 5054-5063, Vol. 22, No. 14
0022-538X/02/$04.00+0     DOI: 10.1128/MCB.22.14.5054-5063.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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