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¹ Department of Biochemistry, Kawasaki Medical School, Kurashiki City, Okayama, Japan
² Central Research Laboratory, Ajinomoto Co. Inc., Suzuki-cho, Kawasaki City, Japan
³ Molecular Biology Laboratory, Department of Biomolecular Science, Faculty of Science, Toho University, Funabashi City, Chiba, Japan
⁴ Department of Human Genetics, University of Utah, Salt Lake City, UT and Biosciences Institute, University College, Cork, Ireland

The maturation/lysis (A2) protein encoded by the group B single-stranded RNA bacteriophage Qß mediates lysis of host Escherichia coli cells. We found a frameshift mutation in the replicase (ß-subunit) gene of Qß cDNA causes cell lysis. The mutant has a single base deletion 73 nucleotides (nt) 3' from the start of the replicase gene with consequent translation termination at a stop codon 129–131 nt further 3'. The 43-amino acid C-terminal part of the 67-amino acid product encoded by what in WT (wild-type) is the +1 frame, is rich in basic amino acids This 67-aa protein can mediate cell lysis whose characteristics indicate that the protein may cause lysis by a different mechanism and via a different target, than that caused by the A2 maturation/lysis protein. Synthesis of a counterpart of the newly discovered lysis product in wild-type phage infection would require a hypothetical ribosomal frameshifting event. The lysis gene of group A RNA phages is also short, 75 codons in MS2, and partially overlaps the first part of their equivalently located replicase gene, raising significant evolutionary implications for the present finding.

Present addresses:^aShowa2-chome, 4-23-1101, Kurashiki City, Okayama, 710-0057, Japan;

^bAminoscience Laboratories, Global Foods & Amino Acids Company, Ajinomoto Co., Inc. 1-1, Suzuki-cho, Kawasaki City, 210-8681, Japan

^* Correspondence: E-mail: tnishihara{at}ma.0038.net