The repressor proteins BlaI and MecI bind similarly to the bla operator imp
licated in the regulation of beta -lactamase synthesis in Staphylococcus au
reus. Dial binds to two separate dyads but neither copper-phenanthroline fo
otprinting nor dimethyl sulphate (DMS) methylation protection assays produc
ed any evidence of a change in the geometry of the DNA between the two dyad
s. It is concluded that BlaI molecules bound at the dyads probably do not c
ause bending or looping of the intervening DNA. DMS protection assays of Bl
aI binding to the bla operator in vitro and in vivo gave similar results so
that it is tentatively concluded that the in vitro results are an accurate
reflection of the in vivo situation. Deletion of the dyad nearest to the b
laZ gene resulted in decreased synthesis of the chloramphenicol acetyltrans
ferase reporter protein synthesized from the blaZ promoter/translation init
itiator. Explanations for this are considered.