G. Condemine et Ve. Shevchik, Overproduction of the secretin OutD suppresses the secretion defect of an Erwinia chrysanthemi outB mutant, MICROBIO-UK, 146, 2000, pp. 639-647
OutB is a component of the Erwinia chrysanthemi Out secretion machinery. Ho
mologues of Outs have been described in two other bacteria. Klebsiella oxyt
oca and Aeromonas hydrophila, but their requirement in the secretion proces
s seems to be different. Study of Outs topology with the BlaM topology prob
e suggests that it is an inner-membrane protein with a large periplasmic do
main. However, fractionation experiments indicate that it could be associat
ed with the outer membrane through its C-terminal part. The secretion defic
iency of an Erw. chrysanthemi outs mutant can be reversed by the addition o
f an inducer of the kdgR regulon. it was shown that this effect results fro
m the increased expression of the secretin OutD and that secretion can be r
estored in an outB mutant by introducing the outD gene on a plasmid. Severa
l experiments suggest an interaction between Outs and OutD. In Erw. chrysan
themi, the presence of OutD stabilizes Outs. OutD expressed in Escherichia
coli can be protected from proteolytic degradation by the coexpression of O
uts. This effect does not require the N-terminal. transmembrane segment of
outB. Outs can be cross-linked with Outs by formaldehyde. These results ind
icate that Outs could act with OutD in the functioning of the Out secretion
machinery.