The R gene product of bacteriophage lambda is the murein transglycosylase |
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Authors: | K Bienkowska-Szewczyk B Lipinska A Taylor |
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Affiliation: | (1) Department of Biochemistry, University of Gdask, Kadki 24, PL-80-822 Gdask, Poland |
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Abstract: | Summary The radioactively labeled proteins synthesised in Escherichia coli minicells infected by bacteriophage R and R+ were compared by polyacrylamide gel electrophoresis. R mutants, which have lost the ability to lyse host cells, lack a polypeptide of molecular weight 17.5 kD corresponding to the molecular weight of murein transglycosylase — a bacteriolytic enzyme from lysates which we have described previously. It has been shown by direct comparison using radio-labeled enzyme that transglycosylase comigrates with the R gene product. The enzyme was endetectable in induced cultures of E. coli W3350 suo (cI857 Ram5) and C600 (cI857 acR301), while it was present in a R–+mutant lysate. We conclude that the transglycosylase is the R gene product.Abbreviations Muropeptide CA GlcNac-1-4-1,6-anhydro-MurNac-L-Ala-D-Glu-msA2pm-D-Ala - muropeptide CB GlcNac-MurNac-GlcNac-1,6-anhydro-MurNac in which the carboxyl groups of MurNac and 1,6-anhydro-MurNac are substituted by the tetrapeptide L-Ala-D-Glu-msA2pm-D-Ala - muropeptide C3 dimer of the two units GlcNac-MurNac-L-Ala-D-Glu-msA2pm-D-Ala which are connected by D-D peptide bond between D-Ala and msA2pm - GlcNac N-acetyl-D-glucosamine - MurNac N-acetylmuramic acid - msA2pm meso-diaminopimelic acid - rivanol 6,9-diamino-2-ethoxyacridine lactate - SDS sodium dodecyl sulfate |
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