Herpes simplex virus defective genomes: structure of HSV-1 ANG defective DNA of class II and encoded polypeptides
| Autor: | Rita Schatten, Charles Knopf, Angelika Otthartmann, Hans Christian Kaerner, Günther Strauss |
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| Rok vydání: | 1983 |
| Předmět: |
Genes
Viral DNA polymerase Concatemer EcoRI Molecular cloning chemistry.chemical_compound Viral Proteins Tandem repeat Virology Simplexvirus Isoelectric Point Gene Genetics biology Base Sequence Defective Viruses DNA Restriction Enzymes Molecular biology DNA-Binding Proteins Molecular Weight Restriction enzyme chemistry DNA Viral biology.protein DNA |
| Zdroj: | The Journal of general virology. 64 |
| ISSN: | 0022-1317 |
| Popis: | Summary Sequence organization and origin of HSV-1 strain Angelotti (ANG) class II defective DNA (HSV-1 ANG dDNA1) were examined in detail by establishing physical maps and by molecular cloning. dDNA1 consists of concatemers of tandem repeat units in which sequences from the U l region spanning map coordinates 0.37 to 0.415 of standard HSV ANG DNA are covalently linked to TR s /IR s sequences. The size of the repeat unit was determined to be about 8.9 kilobase pairs (kb), comprising sequences of 7.3 kb from U l and 1.6 kb from TR s /IR s regions. U l sequences were delineated by restriction enzyme sites KpnI N-P and EcoRI F-M, and were colinear with the corresponding sequences of the standard (wild-type) virus genome. Expression of dDNA1 was studied in African green monkey kidney cells and in Xenopus laevis oocytes. A major polypeptide of approx. mol. wt. 135000 (135K) was overproduced, suggesting that this protein was encoded by dDNA1. By several parameters, e.g. size, immune cross-reactivity, and affinity for native and denatured DNA, the 135K polypeptide was identified as the major HSV DNA-binding protein. It was further shown that the repeat unit contains part of the DNA polymerase gene as demonstrated by its ability to rescue some mutations in this gene. |
| Databáze: | OpenAIRE |
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