ArticleNucleic acids research1998
The protein splicing domain of the homing endonuclease PI-sceI is responsible for specific DNA binding.
Article in Nucleic acids research, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 39 citations in OpenAlex.
- Mitochondrial genome diversity ofFrontiers in microbiology · 2023Article
- Structural Basis for the Propagation of Homing Endonuclease-Associated Inteins.Frontiers in molecular biosciences · 2022Article
- Protein Splicing Activity of theBiochemistry · 2020Article
- Meganucleases and other tools for targeted genome engineering: perspectives and challenges for gene therapy.Current gene therapy · 2011Review
- Evolution of I-SceI homing endonucleases with increased DNA recognition site specificity.Journal of molecular biology · 2011Article
- Mutational analysis of active-site residues in the Mycobacterium leprae RecA intein, a LAGLIDADG homing endonuclease: Asp(122) and Asp(193) are crucial to the double-stranded DNA cleavage activity whereas Asp(218) is not.Protein science : a publication of the Protein Society · 2010Article
- Article
- High resolution crystal structure of domain I of the Saccharomyces cerevisiae homing endonuclease PI-SceI.Nucleic acids research · 2002Article
- Degeneration of a homing endonuclease and its target sequence in a wild yeast strain.Nucleic acids research · 2001Article
- Homing endonucleases: structural and functional insight into the catalysts of intron/intein mobility.Nucleic acids research · 2001Review
- Intronic GIY-YIG endonuclease gene in the mitochondrial genome of Podospora curvicolla: evidence for mobility.Nucleic acids research · 2000Article
- Chimeric restriction enzymes: what is next?Biological chemistryReview
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The homing endonuclease PI- Sce I consists of a protein splicing domain (I) and an endonucleolytic domain (II). To characterize the two domains with respect to their contribution to DNA recognition we cloned, purified and characterized the isolated domains. Both domains have no detectable endonucleolytic activity. Domain I binds specifically to the PI- Sce I recognition sequence, whereas domain II displays only weak non-specific DNA binding. In the specific complex with domain I the DNA is bent to a similar extent as observed with the initial complex formed between PI- Sce I and DNA. Our results indicate that protein splicing domain I is also involved in recognition of the DNA substrate.
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