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Nucleic Acids Research 2005 33(13):e116; doi:10.1093/nar/gni118
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Published online 26 July 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oupjournals.org

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I-ApeI: a novel intron-encoded LAGLIDADG homing endonuclease from the archaeon, Aeropyrum pernix K1

Norimichi Nomura*, Yayoi Morinaga, Nobuaki Shirai1 and Yoshihiko Sako

Division of Applied Biosciences, Graduate School of Agriculture, Kyoto University Kyoto 606-8502, Japan 1Industrial Research Center of Shiga, Ritto-shi Shiga 520-3004, Japan

*To whom correspondence should be addressed. Tel: +81 75 753 6224; Fax: +81 75 753 6226; Email: nom{at}kais.kyoto-u.ac.jp

Received May 8, 2005. Revised June 13, 2005. Accepted June 13, 2005.

Over 50 introns have been reported in archaeal rRNA genes (rDNAs), a subset of which nests putative homing endonuclease (HEase) genes. Here, we report the identification and characterization of a novel archaeal LAGLIDADG-type HEase, I-ApeI, encoded by the ApeK1.S908 intron within the 16S rDNA of Aeropyrum pernix K1. I-ApeI consists of 222 amino acids and harbors two LAGLIDADG-like sequences. It recognizes the 20 bp non-palindromic sequence 5'-GCAAGGCTGAAAC{downarrow}TTAAAGG and cleaves target DNA to produce protruding tetranucleotide 3' ends. Either Mn2+ or Co2+ can be substituted for Mg2+ as a cofactor in the cleavage reaction. Of the 20 bases within the minimal recognition site, 7 are essential for cleavage and are located at positions proximal to the cleavage sites.

The authors wish it to be known that, in their opinion, the first two authors should be regarded as joint First Authors


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