Affiliation:
1. Department of Bacteriology, University of California, Los Angeles, California 90024
Abstract
Treatment with urea-mercaptoethanol of purified spores of
Bacillus thuringiensis
, other
Bacillus
species, and
Clostridium roseum
solubilizes a protein fraction between 5 and 12% of the dry weight of the spores. This fraction behaves identically to the crystal protein of
B. thuringiensis
on acrylamide-gel electrophoresis. The protein from all of the
Bacillus
species shows partial homology with crystal protein, using the Ouchterlony immunodiffusion technique. A further fraction, similar in amount, can be removed from spores of
B. thuringiensis
by the addition of sodium lauryl sulfate to the urea-mercaptoethanol. Spores of
B. thuringiensis
extracted in these ways show no difference when compared to untreated spores with respect to viability or resistance to heat and ultraviolet-irradiation. The extracted spores do show differences in their germination requirements and their susceptibility to phase-darkening by lysozyme. It is concluded that an urea-mercaptoethanol-soluble protein or class of protein is a widespread component of bacterial spores, possibly located in the spore coat, and that this protein may be related to the crystal protein of
B. thuringien
sis.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
37 articles.
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