DsaV methyltransferase and its isoschizomers contain a conserved segment that is similar to the segment in Hhal methyltransferase that is in contact with DNA bases
Open Access
- 1 January 1994
- journal article
- research article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 22 (21) , 4482-4488
- https://doi.org/10.1093/nar/22.21.4482
Abstract
The methyltransferase (MTase) in the DsaV restriction- modification system methylates within 5′-CCNGG sequences. We have cloned the gene for this MTase and determined its sequence. The predicted sequence of the MTase protein contains sequence motifs conserved among all cytosine-5 MTases and is most similar to other MTases that methylate CCNGG sequences, namely M.ScrFI and M.Ssoll. All three MTases methylate the internal cytosine within their recognition sequence. The ‘variable’ region within the three enzymes that methylate CCNGG can be aligned with the sequences of two enzymes that methylate CCWGG sequences. Remarkably, two segments within this region contain significant similarity with the region of M.Hhal that is known to contact DNA bases. These alignments suggest that many cytosine-5 MTases are likely to interact with DNA using a similar structural framework.Keywords
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