The polarity suppression factor of bacteriophage P4 is also a decoration protein of the P4 capsid.
We show that the product of the polarity suppression (psu) gene from bacteriophage P4 associates with P4 capsids. This association can occur when Psu is (i) provided in vivo from the P4 genome or from a plasmid or (ii) provided in vitro by mixing viable phage particles with Psu protein. Psu is unable to associate with the larger capsid of P4's helper phage P2. Discrimination of the P4 and P2 capsids by Psu appears to be independent of the presence of the P4 genome in the capsid, since P2 size capsids filled with P4 DNA cannot accommodate Psu association. P4 psu particles devoid of Psu are less stable than P4 particles carrying Psu. These results indicate that, in addition to its antitermination activity at Rho-dependent terminators, Psu is also a decoration protein that stabilizes the P4 capsids.
Isaksen
M L
ML
Institute of Biology, University of Oslo, Norway.
Rishovd
S T
ST
Calendar
R
R
Lindqvist
B H
BH
D000595:Amino Acid Sequence; D001483:Base Sequence; D002213:Capsid / Q000235:genetics / Q000648:ultrastructure*; D036022:Capsid Proteins; D003090:Coliphages / Q000235:genetics* / Q000254:growth & development / Q000648:ultrastructure; D004279:DNA, Viral / Q000235:genetics; D005814:Genes, Viral; D008969:Molecular Sequence Data; D009154:Mutation; D009838:Oligodeoxyribonucleotides / Q000737:chemistry; D012526:Satellite Viruses / Q000235:genetics*; D015678:Viral Structural Proteins / Q000235:genetics; D014779:Virus Replication
D036022:Capsid Proteins; D004279:DNA, Viral; D009838:Oligodeoxyribonucleotides; D015678:Viral Structural Proteins; C074513:polarity suppression factor, bacteriophage P4