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Nucleic Acids Research, 2002, Vol. 30, No. 17 3839-3847
© 2002 Oxford University Press

Functional analysis of iceA1, a CATG-recognizing restriction endonuclease gene in Helicobacter pylori

Qing Xu1, R. D. Morgan2, R. J. Roberts2, S. Y. Xu2, L. J. van Doorn3, J. P. Donahue4, G. G. Miller1,4 and Martin J. Blaser*,1,4,5

1 Department of Microbiology and Immunology, Vanderbilt University School of Medicine, Nashville, TN 37232, USA, 2 New England Biolabs, Inc., Beverly, MA 01915, USA, 3 Delft Diagnostic Laboratory, Delft, The Netherlands, 4 Division of Infectious Diseases, Department of Medicine, Vanderbilt University School of Medicine and 5 Department of Medicine and Microbiology, New York University School of Medicine, New York, NY 10016, USA

*To whom correspondence should be addressed at: New York University School of Medicine, 550 First Avenue, New York, NY 10016, USA. Tel: +1 212 263 6394; Fax: +1 212 263 7700; Email: martin.blaser{at}med.nyu.edu

iceA1 in Helicobacter pylori is a homolog of nlaIIIR, which encodes the CATG-specific restriction endonuclease NlaIII in Neisseria lactamica. Analysis of iceA1 sequences from 49 H.pylori strains shows that a full-length NlaIII-like ORF is present in 10 strains, including CH4, but in other strains, including strain 60190, the ORFs are truncated due to a variety of mutations. Our goal was to determine whether iceA1 can encode a NlaIII-like endonuclease. Overexpression in Escherichia coli of iceA1 from CH4, but not from 60190, yielded NlaIII-like activity, indicating that the full-length iceA1 is a functional endonuclease gene. Repair of the iceA1 frameshift mutation in strain 60190 and its expression in E.coli yielded functional NlaIII-like activity. We conclude that iceA1 in CH4 is a functional restriction endonuclease gene, while iceA1 in 60190 is not, due to a frameshift mutation, but that its repair restores its restriction endonuclease activity.


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