Nucleotides within both proximal and distal parts of the consensus sequence are important for specific DNA recognition by the herpes simplex virus regulatory protein ICP4
| Autor: | Maggie Elliott, D G Tedder, B. Litman, Roger D. Everett, Lewis I. Pizer |
|---|---|
| Rok vydání: | 1991 |
| Předmět: |
HMG-box
viruses DNA Mutational Analysis Molecular Sequence Data Oligonucleotides Regulatory Sequences Nucleic Acid Methylation Immediate-Early Proteins Single-stranded binding protein Structure-Activity Relationship Viral Envelope Proteins Genetics Consensus sequence Simplexvirus Viral Regulatory and Accessory Proteins Binding Sites Base Sequence biology Binding protein Sequence-Specific DNA Binding Protein DNA-binding domain biochemical phenomena metabolism and nutrition Molecular biology Recombinant Proteins DNA-Binding Proteins DNA binding site biology.protein HeLa Cells Binding domain |
| Zdroj: | Nucleic Acids Research. 19:477-483 |
| ISSN: | 1362-4962 0305-1048 |
| DOI: | 10.1093/nar/19.3.477 |
| Popis: | The herpes simplex virus type 1 regulatory protein ICP4 is a sequence specific DNA binding protein which associates with a number of different sites, some of which include the consensus ATCGTCnnnnYCGRC. In order to investigate the involvement in DNA binding of conserved bases within the consensus, we have synthesised a family of mutant oligonucleotides and tested their ability to form a complex with ICP4. We have also compared the binding specificities of bacterially expressed fragments of ICP4 which include the DNA binding domain. Mutation of most (but not all) bases in the proximal part of the consensus greatly reduced binding by ICP4, as did a mutation affecting the distal part. Most (but not all) G residues identified in methylation interference assays were required for efficient binding. While a bacterially expressed ICP4 peptide encompassing amino acid residues 252-523 bound to DNA with a specificity similar to that of the whole protein, a shorter protein (residues 275-523) had a slightly relaxed DNA binding specificity. |
| Databáze: | OpenAIRE |
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