The final step in the phage infection cycle: the Rz and Rz1 lysis proteins link the inner and outer membranes.
Bacteriophage lambda has four adjacent genes -S, R, Rz and Rz1- dedicated to host cell lysis. While S, encoding the holin and antiholin, and R, encoding the endolysin, have been intensively studied, the products of Rz and Rz1 have not been characterized at either the structural or functional levels. Rz1 is an outer membrane lipoprotein and our results indicate that Rz is a type II signal anchor protein. Here we present evidence that an Rz-Rz1 complex that spans the periplasm carries out the final step in the process of host lysis. These results are discussed in terms of a model where endolysin-mediated degradation of the cell wall is a prerequisite for conformational changes in the Rz-Rz1 complex leading to the juxtaposition and fusion of the IM and OM. Fusion of the two membranes removes the last physical barrier to efficient release of progeny virions.
Berry
Joel
J
Department of Biochemistry and Biophysics, 2128 TAMU, Texas A and M University, College Station TX 77843-2128, USA.
Summer
Elizabeth J
EJ
Struck
Douglas K
DK
Young
Ryland
R
D000595:Amino Acid Sequence; D001433:Bacteriolysis; D010582:Bacteriophage lambda / Q000502:physiology*; D002462:Cell Membrane / Q000378:metabolism*; D008954:Models, Biological; D008969:Molecular Sequence Data; D014764:Viral Proteins / Q000378:metabolism*
D014764:Viral Proteins; C082268:Rz protein, bacteriophage lambda