Subcellular localization of the major pneumococcal autolysin: a peculiar mechanism of secretion in Escherichia coli.
The major pneumococcal autolysin (N-acetylmuramoyl-L-alanine amidase) has been localized in the cellular envelope of Streptococcus pneumoniae and Escherichia coli by using immunocytochemical labeling on ultrathin sections and whole-mounted cells. Cell fractionation experiments in E. coli confirmed the peripheral localization of the pneumococcal amidase and suggested that this enzyme is weakly bound to the outer face of the cytoplasmic membrane. This interaction does not depend on the presence of choline but represents an intrinsic property of the amidase. The autolysin, that is synthesized without any N-terminal signal sequence (García, P., García, J. L., García, E., and López, R. (1986) Gene (Amst.) 43, 265-272) was not processed during translocation. A new regulatory mechanism that might be specific for bacterial autolysins is discussed.
Díaz
E
E
Centro de Investigaciones Biológicas, Consejo Superior de Investigaciones Científicas, Madrid, Spain.
García
E
E
Ascaso
C
C
Méndez
E
E
López
R
R
García
J L
JL
D000581:Amidohydrolases / Q000378:metabolism*; D002462:Cell Membrane / Q000201:enzymology* / Q000648:ultrastructure; D004926:Escherichia coli / Q000201:enzymology* / Q000648:ultrastructure; D008854:Microscopy, Electron; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000032:analysis / Q000378:metabolism*; D013296:Streptococcus pneumoniae / Q000201:enzymology; D013347:Subcellular Fractions / Q000201:enzymology
D000581:Amidohydrolases; D009238:N-Acetylmuramoyl-L-alanine Amidase