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J Biol Chem, Vol. 273, Issue 33, 21217-21224, August 14, 1998
From the a Department of Genetics, In the present studies, we show that the SecD and
SecF equivalents of the Gram-positive bacterium Bacillus
subtilis are jointly present in one polypeptide, denoted SecDF,
that is required to maintain a high capacity for protein secretion.
Unlike the SecD subunit of the pre-protein translocase of
Escherichia coli, SecDF of B. subtilis was not
required for the release of a mature secretory protein from the
membrane, indicating that SecDF is involved in earlier translocation
steps. Strains lacking intact SecDF showed a cold-sensitive phenotype,
which was exacerbated by high level production of secretory proteins,
indicating that protein translocation in B. subtilis is
intrinsically cold-sensitive. Comparison with SecD and SecF proteins
from other organisms revealed the presence of 10 conserved regions in
SecDF, some of which appear to be important for SecDF function.
Interestingly, the SecDF protein of B. subtilis has 12 putative transmembrane domains. Thus, SecDF does not only show sequence
similarity but also structural similarity to secondary solute
transporters. Our data suggest that SecDF of B. subtilis represents a novel type of the SecD and SecF proteins, which seems to
be present in at least two other organisms.
SecDF of Bacillus subtilis, a Molecular Siamese Twin
Required for the Efficient Secretion of Proteins
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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