EcfE, a new essential inner membrane protease: Its role in the regulation of heat shock response in Escherichia coli

Abstract

We have identified a new protease in Escherichia coli, which is required for its viability under normal growth conditions. This protease is anchored in the inner membrane and the gene encoding it has been named ecfE, since it is transcribed by EσE polymerase. Multicopy expression of the ecfE gene was found to turn down expression of both EσE- and Eσ32-transcribed promoters. Purified EcfE degrades both heat shock sigma factors RpoE and RpoH in vitro. EcfE has a zinc binding domain at the N-terminus, a PDZ-like domain in the middle and a highly conserved tripeptide, LDG, at the C-terminus. These features are characteristic of members of a new class of proteases whose activity occurs close to the inner membrane or within the inner membrane. Temperature-sensitive mutants of this gene were isolated mapping to the catalytic site and other domains that exhibited constitutively elevated levels of both heat shock regulons.