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The COOH-terminal Region of pRb2/p130 Binds to Histone Deacetylase 1 (HDAC1), Enhancing Transcriptional Repression of the E2F-dependent Cyclin A Promoter¹

Department of Pathology, Anatomy and Cell Biology, Jefferson Medical College, Philadelphia, Pennsylvania 19107 [P. S., A. D. L., L. B., A. G.], and Laboratory for Cell Metabolism and Pharmacokinetics, CRS, Instituto Regina Elena, Rome, Italy [A. D. L.]

The tumor suppressor retinoblastoma protein family members pRb, p107, and pRb2/p130 are potent negative transcriptional regulators. The best understood target is the transcription factor E2F, which activates cell cycle-dependent transcription of genes controlling and promoting the cell division cycle (e.g., cyclin A). pRb2/p130 is known to be important in implementing cell cycle exit into G₀ due to serum deprivation or various differentiation programs. Several recent studies demonstrated the effect histone acetylases and histone deacetylases (HDACs) have on fine-tuning transcriptional regulation of eucaryotic cells. In this study, we demonstrate that pRb2/p130 binds to HDAC1. This interaction increases the ability of pRb2/p130 to inhibit transcription of the E2F-dependent cyclin A promoter in vivo. We also identify the COOH-terminal 35aa as being necessary for stable interaction between HDAC1 and pRb2/p130.

¹ Supported by NIH grants to A. G. P. S. was supported by the Sbarro Institute for Cancer Research and Molecular Medicine.

² To whom requests for reprints should be addressed, at Department of Pathology, Anatomy and Cell Biology, Room 226, Thomas Jefferson University, 1020 Locust Street, Philadelphia, PA 19107. Fax: (215) 923-9626; E-mail: agiordan@lac.jci.tju.edu.

Received 8/18/98. Accepted 9/24/98.

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