Skip to main content
    • Aa
    • Aa
  • Get access
    Check if you have access via personal or institutional login
  • Cited by 164
  • Cited by
    This article has been cited by the following publications. This list is generated based on data provided by CrossRef.

    Bochtler, Matthias 2016. Indirect DNA Sequence Readout by LAGLIDADG Homing Endonucleases. Structure, Vol. 24, Issue. 6, p. 839.

    Butler, Nathaniel M. and Douches, David S. 2016. Sequence-Specific Nucleases for Genetic Improvement of Potato. American Journal of Potato Research,

    Certo, Michael T. and Morgan, Richard A. 2016. Salient Features of Endonuclease Platforms for Therapeutic Genome Editing. Molecular Therapy,

    Marshall, John M. and Akbari, Omar S. 2016. Genetic Control of Malaria and Dengue.

    Ramirez-Garcés, Diana Camborde, Laurent Pel, Michiel J. C. Jauneau, Alain Martinez, Yves Néant, Isabelle Leclerc, Catherine Moreau, Marc Dumas, Bernard and Gaulin, Elodie 2016. CRN13 candidate effectors from plant and animal eukaryotic pathogens are DNA-binding proteins which trigger host DNA damage response. New Phytologist, Vol. 210, Issue. 2, p. 602.

    Roy, Alexander C. Wilson, Geoffrey G. and Edgell, David R. 2016. Perpetuating the homing endonuclease life cycle: identification of mutations that modulate and change I-TevI cleavage preference. Nucleic Acids Research, p. gkw614.

    Zhang, Likui Huang, Yanchao Xu, Dandan Yang, Lixiang Qian, Kaicheng Chang, Guozhu Gong, Yong Zhou, Xiaojian and Ma, Kesen 2016. Biochemical characterization of a thermostable HNH endonuclease from deep-sea thermophilic bacteriophage GVE2. Applied Microbiology and Biotechnology,

    Zlopasa, Livija Brachner, Andreas and Foisner, Roland 2016. Nucleo-cytoplasmic shuttling of the endonuclease ankyrin repeats and LEM domain-containing protein 1 (Ankle1) is mediated by canonical nuclear export- and nuclear import signals. BMC Cell Biology, Vol. 17, Issue. 1,

    Atwell, Susanna Corwin, Jason A. Soltis, Nicole E. Subedy, Anushryia Denby, Katherine J. and Kliebenstein, Daniel J. 2015. Whole genome resequencing of Botrytis cinerea isolates identifies high levels of standing diversity. Frontiers in Microbiology, Vol. 6,

    Gruber, A. J. Olsen, T. M. Dvorak, R. H. and Cox, M. M. 2015. Function of the N-terminal segment of the RecA-dependent nuclease Ref. Nucleic Acids Research, Vol. 43, Issue. 3, p. 1795.

    Hickman, Alison B. and Dyda, Fred 2015. The casposon-encoded Cas1 protein fromAciduliprofundum booneiis a DNA integrase that generates target site duplications. Nucleic Acids Research, Vol. 43, Issue. 22, p. 10576.

    Jay, Zackary J. and Inskeep, William P. 2015. The distribution, diversity, and importance of 16S rRNA gene introns in the order Thermoproteales. Biology Direct, Vol. 10, Issue. 1,

    Joshi, Amar Grinter, Rhys Josts, Inokentijs Chen, Sabrina Wojdyla, Justyna A. Lowe, Edward D. Kaminska, Renata Sharp, Connor McCaughey, Laura Roszak, Aleksander W. Cogdell, Richard J. Byron, Olwyn Walker, Daniel and Kleanthous, Colin 2015. Structures of the Ultra-High-Affinity Protein–Protein Complexes of Pyocins S2 and AP41 and Their Cognate Immunity Proteins from Pseudomonas aeruginosa. Journal of Molecular Biology, Vol. 427, Issue. 17, p. 2852.

    Kodzius, Rimantas and Gojobori, Takashi 2015. Marine metagenomics as a source for bioprospecting. Marine Genomics, Vol. 24, p. 21.

    Koonin, Eugene V. Dolja, Valerian V. and Krupovic, Mart 2015. Origins and evolution of viruses of eukaryotes: The ultimate modularity. Virology, Vol. 479-480, p. 2.

    Lim, Kwang-Il 2015. Recent advances in developing molecular tools for targeted genome engineering of mammalian cells. BMB Reports, Vol. 48, Issue. 1, p. 6.

    Lu, Chun-Hua and Willner, Itamar 2015. Stimuliresponsive DNA-funktionalisierte Nano- und Mikrocontainer zur schaltbaren und kontrollierten Freisetzung. Angewandte Chemie, Vol. 127, Issue. 42, p. 12380.

    Lu, Chun-Hua and Willner, Itamar 2015. Stimuli-Responsive DNA-Functionalized Nano-/Microcontainers for Switchable and Controlled Release. Angewandte Chemie International Edition, Vol. 54, Issue. 42, p. 12212.

    Overcash, Justin M. Aryan, Azadeh Myles, Kevin M. and Adelman, Zach N. 2015. Understanding the DNA damage response in order to achieve desired gene editing outcomes in mosquitoes. Chromosome Research, Vol. 23, Issue. 1, p. 31.

    Piégu, Benoît Bire, Solenne Arensburger, Peter and Bigot, Yves 2015. A survey of transposable element classification systems – A call for a fundamental update to meet the challenge of their diversity and complexity. Molecular Phylogenetics and Evolution, Vol. 86, p. 90.


Homing endonuclease structure and function

  • Barry L. Stoddard (a1)
  • DOI:
  • Published online: 01 February 2005

Homing endonucleases are encoded by open reading frames that are embedded within group I, group II and archael introns, as well as inteins (intervening sequences that are spliced and excised post-translationally). These enzymes initiate transfer of those elements (and themselves) by generating strand breaks in cognate alleles that lack the intervening sequence, as well as in additional ectopic sites that broaden the range of intron and intein mobility. Homing endonucleases can be divided into several unique families that are remarkable in several respects: they display extremely high DNA-binding specificities which arise from long DNA target sites (14–40 bp), they are tolerant of a variety of sequence variations in these sites, and they display disparate DNA cleavage mechanisms. A significant number of homing endonucleases also act as maturases (highly specific cofactors for the RNA splicing reactions of their cognate introns). Of the known homing group I endonuclease families, two (HNH and His-Cys box enzymes) appear to be diverged from a common ancestral nuclease. While crystal structures of several representatives of the LAGLIDADG endonuclease family have been determined, only structures of single members of the HNH (I-HmuI), His-Cys box (I-PpoI) and GIY-YIG (I-TevI) families have been elucidated. These studies provide an important source of information for structure–function relationships in those families, and are the centerpiece of this review. Finally, homing endonucleases are significant targets for redesign and selection experiments, in hopes of generating novel DNA binding and cutting reagents for a variety of genomic applications.

Corresponding author
Tel.: 1-206-667-4031; Fax: 1-206-667-6877; E-mail:
Recommend this journal

Email your librarian or administrator to recommend adding this journal to your organisation's collection.

Quarterly Reviews of Biophysics
  • ISSN: 0033-5835
  • EISSN: 1469-8994
  • URL: /core/journals/quarterly-reviews-of-biophysics
Please enter your name
Please enter a valid email address
Who would you like to send this to? *