The SPP1 connection

The connector of the virulent Bacillus subtilis bacteriophage SPP1 (Styloviridae) is a structure localized at the phage head vertex which attaches the tail. It is formed by oligomerization of SPP1 gene product 6 (gp6; portal protein). The purified protein is found in solution essentially as a homo‐tredecamer. Its assembly pattern resembles the turbine‐like organization found for other portal proteins and has a defined handedness (Dube et al. (1993) EMBO J. 12, 1303–1309). A preliminary reconstruction of the structure shows that gp6 is composed of a lower ring connected by a narrow region to the upper area consisting of 13 lobes radiating from an inner ring. The assembly is organized around a central channel which spans its full height. A functional characterization of gp6 mutants showed that substitutions of defined amino acids by more basic residues lead to packaging of reduced amounts of DNA into the phage head (Tavares et al. (1992) J. Mol. Biol. 225, 81–92). Since SPP1 encapsidates its DNA by a headful mechanism, these mutations ( siz ) affect most probably a function on the headful sensor—signal transduction—headful cut system. Combination of siz alleles has severe effects in packaging. The resulting gp6 versions lead to the encapsidation of shorter DNA molecules at a lower efficiency than single siz mutants. Gene 6 is expressed late during SPP1 infection. Interestingly, the mass of portal protein inside the cell then increases continuously until lysis, reaching a level several fold higher than the amount required to accomplish its role as a structural component of the virion.