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A set of mutants ofBacillus subtilis bacteriophage φ29 unable to synthesize the head fiber protein has been identified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography. Infectious phage are produced during restrictive infection. We have focused on mutantsus 8.5(900) because the mutation is suppressible by both thesu +3 andsu +44 hosts, and it can be mapped by three- and four-factor crosses. After restrictive infection with mutantsus 8.5(900), a fragment about 70% of the size of the normal fiber is produced as well as particles that are fast-sedimenting in sucrose gradients relative to φ29+ . These particles have the buoyant density of particles with the fibers removed and have the absolute plating efficiency of φ29+ . Fiber protein is absent from prohead as well as virion. A second set of mutants produces fiber protein with a slightly altered electrophoretic mobility. This type of fiber protein is either present or absent on both prohead and virion. A third class of mutants, typified by 914, produces a “normal” fiber, but a major head protein of altered electrophoretic mobility. After infection by this mutant, the fiber is absent from both prohead and virion, and the biological and physical properties of the 914− particle are similar to those of particles produced after infection of thesu − host bysus 8.5(900). These observations suggest that the head fiber is not an essential component of the prohead or virion and that the assembly process is efficient in the absence of fiber protein. Three- and four-factor genetic crosses have established the ordersus 8(769)-8(914)-sus 8.5(900)-sus 9(756) and indicate that cistrons 8 and 8.5 code for the major head protein and head fiber protein, respectively.

Morphogenesis of Bacteriophage φ29 of Bacillus subtilis : Mapping and Functional Analysis of the Head Fiber Gene