Raffaele Ieva

Autoregulation of Helicobacter pylori Fur revealed by functional analysis of the iron-binding site.

The iron-responsive regulator fur is transcriptionally autoregulated and not essential in Neisseria meningitidis.

CrgA is an inducible LysR-type regulator of Neisseria meningitidis, acting both as a repressor and as an activator of gene transcription.

In vitro analysis of protein-operator interactions of the NikR and fur metal-responsive regulators of coregulated genes in Helicobacter pylori.

Incorporation of a polypeptide segment into the beta-domain pore during the assembly of a bacterial autotransporter.

OxyR tightly regulates catalase expression in Neisseria meningitidis through both repression and activation mechanisms.

Interaction of an autotransporter passenger domain with BamA during its translocation across the bacterial outer membrane.

Secretion of a bacterial virulence factor is driven by the folding of a C-terminal segment.

Sequential and spatially restricted interactions of assembly factors with an autotransporter beta domain.

Mgr2 promotes coupling of the mitochondrial presequence translocase to partner complexes.

Mechanistic link between β barrel assembly and the initiation of autotransporter secretion.

Mitochondrial inner membrane protease promotes assembly of presequence translocase by removing a carboxy-terminal targeting sequence.