A teichuronic acid containing rhamnose from cell walls of Bacillus megaterium.
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Biomedical subjects
Publications and source records attributed to C Gilvarg.
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An oligomeric intermediate in the biosynthetic pathway of peptidoglycan was isolated from B. megaterium. The oligomer has been identified as [disaccharide(pentapeptide)]12 pyrophosphoryl undecaprenol.
It has been reported earlier that phage Qbeta RNA (Gilvarg, C., Bollum, F.J. and Weissmann, C. (1975) Proc. Natl. Acad. Sci. U.S. 72, 428-432) elongated at its 3' terminus with up to 100 or more AMP residues retained its full infectivity for Escherichia coli spheroplasts, and that the resulting progeny did not inherit the poly (A) appendage. We now show that while poly (A)-Qbeta RNA appears to function normally as messenger for the synthesis of virus-specific proteins it has lost its capacity to serve as template for Qbeta replicase. Template function could be restored by phosphorolysis with polynucleotide phosphorylase. Taken in conjunction, these results imply that after poly (A)-Qbeta RNA enters the spheroplast a host enzyme (perhaps polynucleotide phosphorylase) removes part or all of the adenylate residues prior to replication of the RNA.
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Terminal riboadenylate transferase, purified from calf thymus, has been used to add a poly(A) extension to the 3' end of Qbeta RNA. The modified Qbeta RNA retains full infectivity in a spheroplast assay system. However, the progeny viruses do not contain poly(A) termini, indicating an in vivo rectification of the in vitro alteration.
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Beta-attenuation analysis of intact spores of Bacillus megaterium containing tritium-labeled dipicolinic acid has shown that dipicolinic acid is located in the spore protoplast and not in the cortex.
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