Impact of peptidoglycan O-acetylation on autolytic activities of the Enterococcus faecalis N-acetylglucosaminidase AtlA and N-acetylmuramidase AtlB.
Autolysins are potentially lethal enzymes that partially hydrolyze peptidoglycan for incorporation of new precursors and septum cleavage after cell division. Here, we explored the impact of peptidoglycan O-acetylation on the enzymatic activities of Enterococcus faecalis major autolysins, the N-acetylglucosaminidase AtlA and the N-acetylmuramidase AtlB. We constructed isogenic strains with various O-acetylation levels and used them as substrates to assay E. faecalis autolysin activities. Peptidoglycan O-acetylation had a marginal inhibitory impact on the activities of these enzymes. In contrast, removal of cell wall glycopolymers increased the AtlB activity (37-fold), suggesting that these polymers negatively control the activity of this enzyme.
Emirian
Aurélie
A
Centre de Recherche des Cordeliers, INSERM U872, 75006 Paris, France.
Fromentin
Sophie
S
Eckert
Catherine
C
Chau
Françoise
F
Dubost
Lionel
L
Delepierre
Muriel
M
Gutmann
Laurent
L
Arthur
Michel
M
Mesnage
Stéphane
S
D000107:Acetylation; D000118:Acetylglucosaminidase / Q000378:metabolism*; D001433:Bacteriolysis; D002473:Cell Wall / Q000737:chemistry; D013293:Enterococcus faecalis / Q000201:enzymology* / Q000502:physiology; D006026:Glycoside Hydrolases / Q000378:metabolism*; D010457:Peptidoglycan / Q000378:metabolism*
D010457:Peptidoglycan; D006026:Glycoside Hydrolases; C026255:endo-N-acetylmuramidase; D000118:Acetylglucosaminidase