The td intron endonuclease I-TevI makes extensive sequence-tolerant contacts across the minor groove of its DNA target
| Autor: | Susan M. Quirk, J. E. Mueller, Marlene Belfort, Mary Bryk, C Lawrence, Nick Loizos |
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| Rok vydání: | 1993 |
| Předmět: |
Molecular Sequence Data
General Biochemistry Genetics and Molecular Biology Phosphates Substrate Specificity Bacteriophage Endonuclease chemistry.chemical_compound Nucleotide Endodeoxyribonucleases Molecular Biology chemistry.chemical_classification Genetics Ethane Base Sequence General Immunology and Microbiology biology General Neuroscience Intron Correction biology.organism_classification Introns Footprinting chemistry DNA Viral Mutation biology.protein Nucleic acid Nucleic Acid Conformation T-Phages DNA Research Article |
| Zdroj: | Scopus-Elsevier |
| ISSN: | 0261-4189 |
| Popis: | I-TevI, a double-strand DNA endonuclease encoded by the mobile td intron of phage T4, has specificity for the intronless td allele. Genetic and physical studies indicate that the enzyme makes extensive contacts with its DNA substrate over at least three helical turns and around the circumference of the helix. Remarkably, no single nucleotide within a 48 bp region encompassing this interaction domain is essential for cleavage. Although two subdomains (DI and DII) contain preferred sequences, a third domain (DIII), a primary region of contact with the enzyme, displays much lower sequence preference. While DII and DIII suffice for recognition and binding of I-TevI, all three domains are important for formation of a cleavage-competent complex. Mutational, footprinting and interference studies indicate predominant interactions of I-TevI across the minor groove and phosphate backbone of the DNA. Contacts appear not to be at the single nucleotide level; rather, redundant interactions and/or structural recognition are implied. These unusual properties provide a basis for understanding how I-TevI recognizes T-even phage DNA, which is heavily modified in the major groove. These recognition characteristics may increase the range of natural substrates available to the endonuclease, thereby extending the invasive potential of the mobile intron. |
| Databáze: | OpenAIRE |
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