Bacteriophage lambda lysis gene product modified and inserted into Escherichia coli outer membrane: Rz1 lipoprotein.

Lysis proteins of bacteriophage lambda were localized in different parts of the host envelope: S in the inner membrane,36 Rz in the membrane adhesion sites,14 and Rz1 in the outer membrane. The R gene product, the transglycosylase destroying bacterial murein, is a soluble protein. Computer-assisted analysis of the Rz1 protein amino acids sequence revealed that its N-terminal part contained the site 15VVVG [symbol: see text] C20, which could be recognizable for the SPase II and cleaved leaving lipid modified C20 as the N-terminal amino acid of the mature protein. Microsequencing of the Rz1 protein isolated from the expression products of E. coli [pSB54] carrying the Rz1 gene showed that the N-terminal part of the protein was cleaved as predicted. Lipid labeling with [3H]palmitate confirmed the expectation that Rz1 was a lipoprotein. E. coli [pSB54] treated with globomycin accumulated prolipoprotein, the Rz1 precursor, which was detectable by the anti-Rz1 serum on electropherograms as the 6.5-kDa protein, larger than mature protein. Physiological function of the Rz1 protein remains to be discovered, but as a first hint we noticed that it evokes increase of the fraction of adhesion sites of outer and inner membranes when overproduced from pSB54. The same effect was observed in induced E. coli (lambda) just before the lysis onset, however, one should be cautious in interpreting the results obtained in conditions of the overproduction of the Rz1 lipoprotein.