@article{mbs:/content/journal/jgv/10.1099/0022-1317-64-11-2455, author = "Knopf, Charles and Strauss, Günther and Otthartmann, Angelika and Schatten, Rita and Kaerner, Hans Christian", title = "Herpes Simplex Virus Defective Genomes: Structure of HSV-1 ANG Defective DNA of Class II and Encoded Polypeptides", journal= "Journal of General Virology", year = "1983", volume = "64", number = "11", pages = "2455-2470", doi = "https://doi.org/10.1099/0022-1317-64-11-2455", url = "https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-64-11-2455", publisher = "Microbiology Society", issn = "1465-2099", type = "Journal Article", keywords = "HSV", keywords = "mapping", keywords = "polypeptides", keywords = "defective DNA", abstract = "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.", }