The class 1 cephalosporinase (CepH) and class 2d oxacillinase (AmpH) from a
n Aeromonas hydrophila clinical isolate, strain T429125, have been cloned a
nd sequenced, Both enzymes are typical of their equivalents in other specie
s of Aeromonas. Both cloned beta -lactamase genes were expressed at a low l
evel in a standard laboratory Escherichia coli strain, but when cloned into
a cre deletion E. coli mutant, they were expressed at significantly higher
levels. Specific disruption of the creB gene resulted in similar increased
levels of beta -lactamase expression, so it was concluded that CreB repres
ses the transcription of ampH and cepH in a cre(+) E. coli strain. The expr
ession of cepH was four times that of ampH in the Delta cre mutant because
of an additional factor encoded on the cloned T429125 chromosomal fragment
containing cepH, This factor was able to trans-activate expression of co-re
sident ampH in the Delta cre mutant such that expression of the two genes w
as approximately equal. The entire cepH-containing fragment was sequenced,
but it contained no genes that were obviously related to any known class of
DNA-binding protein.