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Molecular and Cellular Biology, October 2000, p. 7401-7409, Vol. 20, No. 19
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Transcriptional Repression by Drosophila Methyl-CpG-Binding Proteins

Karim Roder,1 Ming-Shiu Hung,1 Tai-Lin Lee,1 Tzu-Yang Lin,2 Hengyi Xiao,3 Ken-Ichi Isobe,3 Jyh-Lyh Juang,2 and C.-K. James Shen1,*

Institute of Molecular Biology, Academia Sinica, Nankang,1 and Division of Genomic Medicine, National Health Research Institute,2 Taipei, Taiwan, Republic of China, and Department of Basic Gerontology, National Institute for Longevity Sciences, Ogu, Aichi 474-8522, Japan3

Received 6 January 2000/Returned for modification 22 February 2000/Accepted 6 July 2000

C methylation at genomic CpG dinucleotides has been implicated in the regulation of a number of genetic activities during vertebrate cell differentiation and embryo development. The methylated CpG could induce chromatin condensation through the recruitment of histone deacetylase (HDAC)-containing complexes by methyl-CpG-binding proteins. These proteins consist of the methylated-DNA binding domain (MBD). Unexpectedly, however, several studies have identified MBD-containing proteins encoded by genes of Drosophila melanogaster, an invertebrate species supposed to be void of detectable m5CpG. We now report the genomic structure of a Drosophila gene, dMBD2/3, that codes for two MBD-containing, alternatively spliced, and developmentally regulated isoforms of proteins, dMBD2/3 and dMBD2/3Delta . Interestingly, in vitro binding experiments showed that as was the case for vertebrate MBD proteins, dMBD2/3Delta could preferentially recognize m5CpG-containing DNA through its MBD. Furthermore, dMBD2/3Delta as well as one of its orthologs in mouse, MBD2b, could function in human cells as a transcriptional corepressor or repressor. The activities of HDACs appeared to be dispensable for transcriptional repression by dMBD2/3Delta . Finally, dMBD2/3Delta also could repress transcription effectively in transfected Drosophila cells. The surprisingly similar structures and characteristics of the MBD proteins as well as DNA cytosine (C-5) methyltransferase-related proteins in Drosophila and vertebrates suggest interesting scenarios for their roles in eukaryotic cellular functions.

* Corresponding author. Mailing address: Institute of Molecular Biology, Academia Sinica, Nankang, Taipei, Taiwan, Republic of China. Phone: 011-886-2-27821436. Fax: 011-886-2-2788-4177. E-mail: ckshen{at}ccvax.sinica.edu.tw or cjshen{at}ucdavis.edu.

Molecular and Cellular Biology, October 2000, p. 7401-7409, Vol. 20, No. 19
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

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