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Nucleic Acids Research, 1992, Vol. 20, No. 23 6267-6273
© 1992

MOLECULAR BIOLOGY

Structure and evolution of the Xcyl restriction-modification system

Barbara E. Withers, Linda A. Ambroso and Joan C. Dunbar*

Wayne State University School of Medicine Detroit, MI 48201, USA

*To whom correspondence should be addressed

Received September 4, 1992. Revised October 27, 1992. Accepted October 27, 1992.

The Xcyl restriction-modification system from Xanthomonas cyanopsidis recognizes the sequence, CCCGGG. The Xcyl endonuclease and methylase genes have been cloned and sequenced and were found to be aligned in a head to tail orientation with the methylase preceding and overlapping the endonuclease by one base pair. The nucleotide sequence codes for an N4 cytosine methyltransferase with a predicted molecular weight of 33,500 and an endonuclease comprised of 333 codons and a molecular weight of 36,600. Sequence comparisons revealed significant similarity between the Xcyl, Cfrl and Smal methylisomers. In contrast, no similarity was detected between the primary structures of the Xcyl and Smal endonucleases. The Xcyl restriction-modification system is highly homologous to the Xmal genes, although the DNA sequences flanking the genes rapidly diverge. The sequence of the Xcyl endonuclease contains two motifs which have recently been identified as essential to the activity of the EcoRV endonuclease.


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