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

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A site-specific endonuclease encoded by a typical archaeal intron. / Dalgaard, Jacob; Garrett, Roger Antony; Belfort, Malene.

In: Proceedings of the National Academy of Science of the United States of America, Vol. 90, No. 12, 1993, p. 5414-5417.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Dalgaard, J, Garrett, RA & Belfort, M 1993, 'A site-specific endonuclease encoded by a typical archaeal intron.', Proceedings of the National Academy of Science of the United States of America, vol. 90, no. 12, pp. 5414-5417.

APA

Dalgaard, J., Garrett, R. A., & Belfort, M. (1993). A site-specific endonuclease encoded by a typical archaeal intron. Proceedings of the National Academy of Science of the United States of America, 90(12), 5414-5417.

Vancouver

Dalgaard J, Garrett RA, Belfort M. A site-specific endonuclease encoded by a typical archaeal intron. Proceedings of the National Academy of Science of the United States of America. 1993;90(12):5414-5417.

Author

Dalgaard, Jacob ; Garrett, Roger Antony ; Belfort, Malene. / A site-specific endonuclease encoded by a typical archaeal intron. In: Proceedings of the National Academy of Science of the United States of America. 1993 ; Vol. 90, No. 12. pp. 5414-5417.

Bibtex

@article{e86af41074ce11dbbee902004c4f4f50,
title = "A site-specific endonuclease encoded by a typical archaeal intron.",
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.",
author = "Jacob Dalgaard and Garrett, {Roger Antony} and Malene Belfort",
year = "1993",
language = "English",
volume = "90",
pages = "5414--5417",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
publisher = "The National Academy of Sciences of the United States of America",
number = "12",

}

RIS

TY - JOUR

T1 - A site-specific endonuclease encoded by a typical archaeal intron.

AU - Dalgaard, Jacob

AU - Garrett, Roger Antony

AU - Belfort, Malene

PY - 1993

Y1 - 1993

N2 - 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.

AB - 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.

M3 - Journal article

VL - 90

SP - 5414

EP - 5417

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 12

ER -

ID: 270289