title: The three-for-one model for gram-negative wall growth: a problem and a possible solution.
abstract: The murein wall in Gram-negative bacteria is so thin that the mechanism of growth is necessarily complicated. From analytical data of murein components, Höltje suggested a model for the growth mechanism that would lead to safe wall enlargement. The model depended on the formation of trimers of peptidoglycan disaccharides linked via their pentapeptides. In the 'three-for-one' model three oligopeptidoglycan chains are linked to each other in the usual linkages between the carboxyl group of D-alanine residues and the epsilon-amino group of diaminopimelic acid residues; these are designated 'tail-to-tail' linkages. This three-chained raft is then linked to the stress-bearing wall via the formation of trimers, defined as three peptide chains linked together by tail-to-tail linkages. Then by autolyzing the oldest bonds in each trimer, the old chain is excised and the raft becomes part of the stress-bearing wall and the wall is enlarged. There is a problem with the three-for-one model in that it demands a precise fitting of the prefabricated raft of three crosslinked chains to a stress-bearing chain in the wall fabric to allow the series of trimer linkages to form. Because the wall, when bearing stress, must be pulled into a 'honeycomb' structure, the end-to-end distance would be shortened. The possibility is raised here that the glycan chains in the stress-bearing wall are stretched to a sufficient degree by the cell's turgor pressure to compensate for its zig-zag structure; this could allow the model to function. A calculation is presented that assumes that the area of the pores in the fabric, called tessera, is maximized by the cell's turgor pressure. In this case the glycan chain must stretch 10% (and the end-to-end distance of peptide strands stretch 28%) so that the end-to-end distance of a glycan chain in the stress-bearing wall and the unstretched nascent wall can be the same and permit indefinite stable growth.
authors.affiliation: Biology Department, Indiana University, Bloomington 47405, USA. Koch@indiana.edu
authors.forename: A L
authors.initials: AL
authors.lastname: Koch
mesh_terms: D002240:Carbohydrate Sequence; D002473:Cell Wall / Q000737:chemistry*; D006090:Gram-Negative Bacteria / Q000737:chemistry*; D008956:Models, Chemical; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry; D010457:Peptidoglycan / Q000737:chemistry
chemical_list: D009842:Oligopeptides; D010457:Peptidoglycan