Abstract
SUMMARY: A regular array exhibiting hexagonal periodicity with a centre-to-centre spacing of about 6 nm was found on the wall surface of freeze-etched Lactobacillus buchneri. The regular array was composed of a subunit protein with a molecular weight of about 55000 as determined by sodium dodecyl sulphate-polyacrylamide gel electrophoresis. Subunits isolated from the wall by extraction with guanidine hydrochloride reassembled into the original regular array after dialysis against distilled water. The subunits could reattach to wall fragments from which most of the teichoic acid had been extracted with cold trichloroacetic acid, but not to wall fragments from which most of the neutral polysaccharide had been removed by treatment with hot formamide. Heterologous reattachment of the subunits took place on to Lactobacillus casei subsp. casei wall fragments which had been partially hydrolysed under mild acid conditions. These observations suggest that the subunit protein binds to a neutral polysaccharide moiety in the underlying wall layer but not to peptidoglycan or teichoic acid.
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