ArticleNucleic acids research2000
Purification and characterization of the DNA cleavage and recognition site of I-ScaI mitochondrial group I intron encoded endonuclease produced in Escherichia coli.
Article in Nucleic acids research, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Revealing the high variability on nonconserved core and mobile elements of Austropuccinia psidii and other rust mitochondrial genomes.PloS one · 2021Article
- The mitochondrial LSU rRNA group II intron of Ustilago maydis encodes an active homing endonuclease likely involved in intron mobility.PloS one · 2012Article
- Degenerated recognition property of a mitochondrial homing enzyme in the unicellular green alga Chlamydomonas smithii.Plant molecular biology · 2006Article
- Intragenic suppressors that restore the activity of the maturase encoded by the second intron of the Saccharomyces cerevisiae cyt b gene.Current genetics · 2004Article
- Genetic conservation versus variability in mitochondria: the architecture of the mitochondrial genome in the petite-negative yeast Schizosaccharomyces pombe.Current genetics · 2003Review
- An in vivo selection system for homing endonuclease activity.Nucleic acids research · 2002Article
- Homing endonucleases: structural and functional insight into the catalysts of intron/intein mobility.Nucleic acids research · 2001Review
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Authors and funding
4 authors.
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Abstract
The second intron in the mitochondrial cytb gene of Saccharomyces capensis, belonging to group I, encodes a 280 amino acid protein containing two LAGLIDADG motifs. Genetic and molecular studies have previously shown that this protein has a dual function in the wild-type strain. It acts as a specific homing endonuclease I- Sca I promoting intron mobility and as a maturase promoting intron splicing. Here we describe the synthesis of a universal code equivalent to the mitochondrial sequence coding for this protein and the in vitro characterization of I- Sca I endonuclease activity, using a truncated mutant form of the protein p28bi2 produced in Escherichia coli. We have also determined the cleavage pattern as well as the recognition site of p28bi2. It was found that p28bi2 generates a double-strand cleavage downstream from the intron insertion site with 4 nt long 3'-overhangs. Mutational analysis of the DNA target site shows that p28bi2 recognizes a 16-19 bp sequence from positions -11 to +8 with respect to the intron insertion site.
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