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The morphology of Safferman's virus of blue-green algae (phycovirus LPP-1) has been studied by electron microscopy and physicochemical methods. The virion has a short (100 to 200 A long, 150 A in diameter) forked tail, with an outer sheath, an inner core, and a capital attached to one of the vertices of a polyhedral head. The head capsid edge-to-edge distance is 600 A, based upon internal calibration of the magnification in electron micrographs by use of the line-line spacing of catalase crystals. Measurements of absorbancy and infectivity, and electron microscopy across the band of virus after zone centrifugation on a sucrose gradient, indicated that infectivity was correlated with the short-tailed particles described. The viral deoxyribonucleic acid (DNA) is linear, with a contour length of 13.2 +/- 0.5 mu, measured by the Kleinschmidt method. Its sedimentation coefficient, S(0) (20, w), is 33.4 +/- 0.7 S. These values are consistent with a molecular weight of 27 x 10(6) for the viral DNA. Based upon buoyant density in CsCl and thermal denaturation, the guanine-cytosine content of the DNA is 53%. The viral DNA was used as template for in vitro ribonucleic acid (RNA) synthesis by Escherichia coli RNA polymerase. This RNA annealed to 18% of the sequences in the viral DNA, 0.5% of the sequences in bacteriophage T7 DNA, and 0.25% of the sequences in Plectonema boryanum DNA, at saturating levels of RNA in the Hall-Nygaard hybridization assay. The lack of homology with T7 DNA is of interest because the two viruses are very similar morphologically. The lack of homology with host DNA suggests that this algal virus is a poor candidate for transduction.

The structural proteins of mature LPP-1 particles and the patterns of protein synthesis after LPP-1 infection have been examined by electrophoresis on sodium dodecyl sulfate polyacrylamide gels. Structural proteins account for 35% of the LPP-1 genome, and proteins that would require about 65% of the total coding capacity have been detected after infection. The major head proteins have molecular weights of 39,000 and 13,000, whereas the major tail protein is an 80,000-molecular-weight species. Host protein synthesis is depressed soon after infection and appears to be entirely shut off by 5 hr. Three classes of viral proteins are distinguished in infected cells, based on their time course of synthesis and their presence in mature virions.

Endogenous dark respiration in the blue-green alga Plectonema boryanum is markedly affected by preincubation in the light: it can be increased from a basal rate of 5 nmoles of O(2) to 55 nmoles of O(2) per mg of cell protein per min after exposure of the cells to light for 8 to 10 hr. Under conditions of enhanced dark respiration, cyanophage multiplication in the dark increases drastically and approaches the cyanophage yields obtained in photosynthesizing Plectonema cells. This implies that the biosynthetic capabilities of the algal cells, at least with respect to viral synthesis, can be similar in the dark to those in the light. The enhanced endogenous respiration rate was found to be dependent on photoassimilation of CO(2) and on protein synthesis. The implications of these findings with respect to obligate photoautotrophic metabolism in blue-green algae are discussed.

Purified wound tumor virus was found to possess an associated ribonucleic acid (RNA) transcriptase. The product of transcriptase synthesis was shown to be single-stranded RNA which annealed specifically to wound tumor viral RNA.