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Molecular and Cellular Biology, January 2003, p. 250-258, Vol. 23, No. 1
0270-7306/03/$08.00+0     DOI: 10.1128/MCB.23.1.250-258.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Human MI-ER1 Alpha and Beta Function as Transcriptional Repressors by Recruitment of Histone Deacetylase 1 to Their Conserved ELM2 Domain

Zhihu Ding, Laura L. Gillespie, and Gary D. Paterno*

Terry Fox Cancer Research Laboratories, Division of Basic Medical Sciences, Faculty of Medicine, Memorial University of Newfoundland, St. John's, Newfoundland, Canada A1B 3V6

Received 20 May 2002/ Returned for modification 27 June 2002/ Accepted 2 October 2002

mi-er1 (previously called er1) was first isolated from Xenopus laevis embryonic cells as a novel fibroblast growth factor-regulated immediate-early gene. Xmi-er1 was shown to encode a nuclear protein with an N-terminal acidic transcription activation domain. The human orthologue of mi-er1 (hmi-er1) displays 91% similarity to the Xenopus sequence at the amino acid level and was shown to be upregulated in breast carcinoma cell lines and tumors. Alternative splicing at the 3' end of hmi-er1 produces two major isoforms, hMI-ER1{alpha} and hMI-ER1ß, which contain distinct C-terminal domains. In this study, we investigated the role of hMI-ER1{alpha} and hMI-ER1ß in the regulation of transcription. Using fusion proteins of hMI-ER1{alpha} or hMI-ER1ß tethered to the GAL4 DNA binding domain, we show that both isoforms, when recruited to the G5tkCAT minimal promoter, function to repress transcription. We demonstrate that this repressor activity is due to interaction and recruitment of a trichostatin A-sensitive histone deacetylase 1 (HDAC1). Furthermore, deletion analysis revealed that recruitment of HDAC1 to hMI-ER1{alpha} and hMI-ER1ß occurs through their common ELM2 domain. The ELM2 domain was first described in the Caenorhabditis elegans Egl-27 protein and is present in a number of SANT domain-containing transcription factors. This is the first report of a function for the ELM2 domain, highlighting its role in the regulation of transcription.

* Corresponding author. Mailing address: Terry Fox Cancer Research Laboratories, Division of Basic Medical Sciences, Faculty of Medicine, Memorial University, St. John's, Newfoundland, Canada A1B 3V6. Phone: (709) 777-7012. Fax: (709) 777-7010. E-mail: gpaterno{at}mun.ca.

Molecular and Cellular Biology, January 2003, p. 250-258, Vol. 23, No. 1
0022-538X/03/$08.00+0     DOI: 10.1128/MCB.23.1.250-258.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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