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  Excision of the doubly methylated base N-4,5-dimethylcytosine from DNA by Escherichia coli Nei and Fpg proteins.

Alexeeva, M., Guragain, P., Tesfahun, A. N., Tomkuviene, M., Arshad, A., Gerasimaite, R., et al. (2018). Excision of the doubly methylated base N-4,5-dimethylcytosine from DNA by Escherichia coli Nei and Fpg proteins. Philosophical Transactions of the Royal Society B: Biological Sciences, 373(1748): 20170337. doi:10.1098/rstb.2017.0337.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0001-4141-C Version Permalink: http://hdl.handle.net/21.11116/0000-0003-29D9-B
Genre: Journal Article

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 Creators:
Alexeeva, M., Author
Guragain, P., Author
Tesfahun, A. N., Author
Tomkuviene, M., Author
Arshad, A., Author
Gerasimaite, R.1, Author              
Rugenaite, A., Author
Urbanaviciute, G., Author
Bjoras, M., Author
Laerdahl, J. K., Author
Klungland, A., Author
Klimasauskas, S., Author
Bjelland, S., Author
Affiliations:
1Department of Cellular Logistics, MPI for Biophysical Chemistry, Max Planck Society, ou_578574              

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Free keywords: 5-methylcytosine methylation damage; DNA base excision repair; N-4,5-dimethylcytosine; epigenetics
 Abstract: Cytosine (C) in DNA is often modified to 5-methylcytosine (m(5)C) to execute important cellular functions. Despite the significance of m(5)C for epigenetic regulation in mammals, damage to m(5)C has received little attention. For instance, almost no studies exist on erroneous methylation of m(5)C by alkylating agents to doubly or triply methylated bases. Owing to chemical evidence, and because many prokaryotes express methyltransferases able to convert m(5)C into N-4,5-dimethylcytosine (m(N4,5)C) inDNA, m(N4,5)C is probably present in vivo. We screened a series of glycosylases from prokaryotic to human and found significant DNA incision activity of the Escherichia coli Nei and Fpg proteins at m(N4,5)C residues in vitro. The activity of Nei was highest opposite cognate guanine followed by adenine, thymine (T) and C. Fpg-complemented Nei by exhibiting the highest activity opposite C followed by lower activity opposite T. To our knowledge, this is the first description of a repair enzyme activity at a further methylated m(5)C in DNA, as well as the first alkylated base allocated as a Nei or Fpg substrate. Based on our observed high sensitivity to nuclease S1 digestion, we suggest that m(N4,5)C occurs as a disturbing lesion inDNA and that Nei may serve as a major DNA glycosylase in E. coli to initiate its repair.

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Language(s): eng - English
 Dates: 2018-04-232018-06-05
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1098/rstb.2017.0337
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Title: Philosophical Transactions of the Royal Society B: Biological Sciences
Source Genre: Journal
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Pages: 8 Volume / Issue: 373 (1748) Sequence Number: 20170337 Start / End Page: - Identifier: -