Reassembly of a regularly arranged protein in the cell wall of Lactobacillus buchneri and its reattachment to cell walls: chemical modification studies.

Regularly arranged protein (RA protein) isolated from the cell wall of Lactobacillus buchneri was chemically modified by amidination, acetylation, succinylation, and amidation. The modified RA proteins were examined for their ability to reassemble into a regular array and to reattach to the cell walls from which the regular array had been detached. Only amidinated RA protein could be either reassembled into a regular array or reattached to the cell walls; RA proteins modified by the other methods lost the ability for both reassembly and reattachment. The unmodified RA protein could be reattached to periodate-oxidized cell walls, but not to methylated ones. These results suggest that the positive charge of the amino group as well as the negative charge of the carboxyl group of RA protein plays an important role(s) in morphogenesis of the hexagonal array and in its attachment to the underlying cell wall layer. The periodate-insensitive lone hydroxyl groups of the neutral polysaccharide molecule in the cell wall seem to be the receptor sites for RA protein in the attachment to the cell wall.