We report the complete DNA sequence of the short repeat region in the genome of herpes simplex virus type 1, as 6633 base pairs of composition 79.5% G+C. This contains immediate early gene 3, encoding the IE175 protein, an important transcriptional activator of later virus genes. The IE175 coding region was identified as a 3894 base sequence of 81.5% G+C DNA. The base composition of this gene is thus the most extreme yet determined, and the IE175 predicted amino acid composition is correspondingly biased, most notably with an alanine content of 20.9%. Functionally important regions of the IE175 polypeptide were tentatively identified by comparison with the sequence of the homologous protein from varicella-zoster virus and from locations of ts mutations, and were correlated with properties of the amino acid sequence. Aspects of the evolution of such an extreme composition DNA sequence were discussed.

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In rabbit kidney cells infected with strains of Herpes simplex virus producing either cell-rounding or polycaryocytosis. Vinblastine induced paracrystals. This could be shown by phase-contrast- and electron-microscopy. Infections were done under one-step-growth conditions or at low MOI. 90 per cent noninfected cells contained stress fibers as detected by Servablue R250-staining. Shortly after recruitment into polycaryocytes, stress fibres of normal length appearing in criss-cross arrangement can be seen in the periphery of these cells. Later they polymerize to very long fibers and finally they are partially destroyed. The time of destruction depends on the MOI employed. By using Actinomycin D and/or Cycloheximide as blocking agents, it could be shown that polymerization of microfilaments correlates in time with giant cell formation. In view of the fact that the virus synthesis is accompanied in parallel by a special rearrangement of microfilaments as well as polycaryocytosis, both these processes have to be considered as caused by early (and late ?) protein-synthesis (beta-/gamma-proteins) but not as induced by "very-early" proteins (alpha-proteins).

SUMMARYBHK (dPyK-) cells infected with herpes simplex virus type 1 (HSV-1) contain a virus-induced deoxythymidine (dThd)-phosphorylating enzyme. This enzyme uses AMP as phosphate donor and is called AMP:deoxythymidine 5'-phosphotransferase (or kinase). The enzyme was purified over 1300-fold and was found to be specific for an AMP substrate. It can thus be distinguished from virus-specific deoxypyrimidine kinase (dPyK). It was shown that the two substrates AMP and dThd participate in the reaction at a 1 : 1 molar ratio; the K m for AMP was 2.3 gM and for dThd it was 2, 1 #M. The mol. wt. of the enzyme was estimated to be between 110000 (by glycerol gradient centrifugation) and 90000 (by gel filtration). For optimum activity, the phosphotransferase required an alkaline pH, and 37 °C; the activation energy of the reaction was 18 450 cal/mol. The appearance of the enzyme after infection parallels that of viral DNA synthesis-related functions.

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