Characterization of MeCP2, a vertebrate DNA binding protein with affinity for methylated DNA (original) (raw)
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Institute of Cell and Molecular Biology, University of Edinburgh
Kings Buildings, Edinburgh EH9 3JR, UK
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Institute of Cell and Molecular Biology, University of Edinburgh
Kings Buildings, Edinburgh EH9 3JR, UK
- Present address: Gene expression, European Molecular Biology Laboratory, D6900, Heidelberg, Germany
Search for other works by this author on:
Institute of Cell and Molecular Biology, University of Edinburgh
Kings Buildings, Edinburgh EH9 3JR, UK
Search for other works by this author on:
- Present address: Gene expression, European Molecular Biology Laboratory, D6900, Heidelberg, Germany
Revision received:
08 September 1992
Accepted:
08 September 1992
Published:
11 October 1992
Cite
Richard Meehan, Joe D. Lewis, Adrian P. Bird, Characterization of MeCP2, a vertebrate DNA binding protein with affinity for methylated DNA, Nucleic Acids Research, Volume 20, Issue 19, 11 October 1992, Pages 5085–5092, https://doi.org/10.1093/nar/20.19.5085
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Abstract
Methylated DNA in vertebrates is associated with transcriptional repression and inactive chromatin. Two activities have been identified, MeCP1 and MeCP2, which bind specifically to DNA containing methyl-CpG pairs. In this report we characterize MeCP2. We show that it is more abundant than MeCP1, is more tightly bound in the nucleus, and is distinguishable chromatographically. The two proteins share widespread expression in somatic mammalian cells, and barely detectable expression in early embryonic cells. DNAs containing thymidine which has a methyl group at position 5 are not ligands for the MeCPs. The possible role of MeCP2 in methylatlon-associated gene inactivatJon was tested in in vitro transcription extracts. Purified MeCP2 inhibited transcription from both methylated and nonmethylated DNA templates in vitro , probably due to the presence of nonspecific DNA binding domains within the protein. We hypothesise that MeCP2 normally binds methylated DNA in the context of chromatin, contributing to the long-term repression and nuclease-resistance of methyl-CpGs.
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Author notes
- Present address: Gene expression, European Molecular Biology Laboratory, D6900, Heidelberg, Germany
© 1992 Oxford University Press
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