ISSN:
1574-6968
Source:
Blackwell Publishing Journal Backfiles 1879-2005
Topics:
Biology
Notes:
Abstract The lytic enzyme from bacteriophage ψM1-induced lysates of Methanobacterium thermoautotrophicum was purified approx. 80-fold to near electrophoretic homogeneity. It was a 31-kDa monomeric, oxygen-sensitive pseudomurein endopeptidase hydrolysing the ?-Ala-Lys bond of pseudomurein. Pseudomurein endopeptidase-specific polyclonal antibodies reacted with a 31-kDa protein in crude extracts of non-infected host cells. This cross-reacting protein was purified. It did not exhibit lytic activity but its N-terminus was identical with the N-terminus of pseudomurein endopeptidase. The 31-kDa protein thus probably represents a pseudomurein endopeptidase whose autolytic activity is under control in non-infected, but deregulated in phage ψM1-infected cells. Its preferential location in the cell-wall area was demonstrated by immuno-electron microscopy and argued for a role of pseudomurein endopeptidase in the expansion of the cell wall during growth.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1111/j.1574-6968.1992.tb14073.x
