A site-specific endonuclease encoded by a typical archaeal intron.

Jacob Dalgaard, Roger Antony Garrett, Malene Belfort

81 Citations (Scopus)

Abstract

The protein encoded by the archaeal intron in the 23S rRNA gene of the hyperthermophile Desulfurococcus mobilis is a double-strand DNase that, like group I intron homing endonucleases, is capable of cleaving an intronless allele of the gene. This enzyme, I-Dmo I, is unusual among the intron endonucleases in that it is thermostable and is expressed only from linear and cyclized intron species and not from the precursor RNA. However, in analogy to its eukaryotic counterparts, but unlike the bacteriophage enzymes, I-Dmo I makes a staggered double-strand cut that generates 4-nt 3' extensions. Additionally, although the archaeal and group I introns have entirely different structural properties and splicing pathways, I-Dmo I shares sequence similarity, in the form of the LAGLI-DADG motif, with group I intron endonucleases of eukaryotes. These observations support the independent evolutionary origin of endonucleases and intron core elements and are consistent with the invasive potential of endonuclease genes.
Original languageEnglish
JournalProceedings of the National Academy of Science of the United States of America
Volume90
Issue number12
Pages (from-to)5414-5417
ISSN0027-8424
Publication statusPublished - 1993

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