Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/47134
Título : Structure and assembly of phage phi29.
Autor : Viñuela, Eladio, Camacho, Ana Gema, Jimenez, F., Carrascosa, José L., Ramírez, G., Salas, Margarita
Palabras clave : Phi29
Bacteriophage
Mutations
Non-structural protein
Fecha de publicación : 1976
Editor: Royal Society (Great Britain)
Resumen: Bacteriophage phi29 is a small, morphologically complex, virus with a DNA of molecular mass 12 X 10(6). The most likely structure of the head of phi29 consists of two fivefold symmetric end-caps based on T = 1 icosahedral symmetry, separated by an equatorial row of 5 hexamers. The eighteen genes identified in phi29 genome have been mapped and, in some cases, the gene products have been identified. Five linked genes, four coding for structural proteins (G, A, E, H) and one coding for a non-structural protein (J), are essential to determine the normal shape of the capsid. Protein pJ may be a scaffolding protein. An account of the effects of mutations in phi29 genes is given.
Versión del editor: http://dx.doi.org/10.1098/rstb.1976.0095
URI : http://hdl.handle.net/10261/47134
ISSN: 1471-2970
Citación : Proceedings of the Royal Society of London - B
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