Autolytic formation of protoplasts (autoplasts) of Streptococcus faecalis; location of active and latent autolysin.
Over 80% of the active and porteinase-activatable, latent forms of the autolytic N-acetylmuramide glycanhydrolase of Streptococcus faecalis ATCC 9790 were released to the supernatant buffer during the autolytic formation of protoplasts (autoplasts) in the presence of absence of trypsin. Autolysin activity was not found in association with released mesosomal vesicles and had little affinity for binding to membranes or to the outer surface of the wall. Isolated walls were able to bind over four times as much autolysin activity as that present on wall exponential-phase cells. Using a rapid technique for wall isolation, evidence was obtained that the latent form (as well as the active form) was wall bound in intact cells. In addition, isotope labeling and ultrastructural studies were able to show that latent autolysin was concentrated in the newer, septally associated portion of the wall.
D001433:Bacteriolysis; D001665:Binding Sites; D002458:Cell Fractionation; D002473:Cell Wall / Q000201:enzymology / Q000378:metabolism; D013293:Enterococcus faecalis / Q000201:enzymology* / Q000378:metabolism / Q000648:ultrastructure; D006026:Glycoside Hydrolases / Q000032:analysis* / Q000378:metabolism; D008566:Membranes / Q000378:metabolism; D009112:Muramic Acids; D011523:Protoplasts
D009112:Muramic Acids; D006026:Glycoside Hydrolases