SUMMARY: The distribution of muropeptides formed by muramidase digestion of peptidoglycan from H was determined by gel-filtration HPLC. The observed crosslinking pattern supports the conclusion that incorporation of peptidoglycan in proceeds by a similar mechanism to that proposed earlier for In this mechanism single glycan-peptide strands are incorporated into the sacculus by crosslinking reactions that take place only between the monomer muropeptide units of the incoming glycopeptide and muropeptides present in the innermost region of wall at the wall-membrane interface: such crosslinking reactions take place only during incorporation and no other crosslinking reactions occur. This assembly process has now been termed restricted monomer addition. The present analysis shows that the distribution of muropeptides in peptidoglycan is in excellent agreement with that predicted by this mechanism. We propose that cell wall assembly in proceeds via restricted monomer addition without any requirement for the secondary crosslinking reactions that have been suggested to occur in this organism. The high degree of crosslinking in 80% in this study, may result mainly from the freedom for crosslinking provided by the pentaglycine bridge peptide.


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