Donald B. Oliver

Lyme disease-causing Borrelia species encode multiple lipoproteins homologous to peptide-binding proteins of ABC-type transporters.

Regulation of Escherichia coli secA by cellular protein secretion proficiency requires an intact gene X signal sequence and an active translocon.

Characterization of Borrelia burgdorferi BlyA and BlyB proteins: a prophage-encoded holin-like system.

Translocon "pulling" of nascent SecM controls the duration of its translational pause and secretion-responsive secA regulation.

Role of a conserved glutamate residue in the Escherichia coli SecA ATPase mechanism.

In vivo membrane topology of Escherichia coli SecA ATPase reveals extensive periplasmic exposure of multiple functionally important domains clustering on one face of SecA.

Mapping of the signal peptide-binding domain of Escherichia coli SecA using Förster resonance energy transfer.

Mapping of the SecA·SecY and SecA·SecG interfaces by site-directed in vivo photocross-linking.

Characterization of the Escherichia coli SecA signal peptide-binding site.

The variable subdomain of Escherichia coli SecA functions to regulate SecA ATPase activity and ADP release.

Defining the solution state dimer structure of Escherichia coli SecA using Förster resonance energy transfer.

Determination of the Oligomeric State of SecYEG Protein Secretion Channel Complex Using in Vivo Photo- and Disulfide Cross-linking.

The SecA protein deeply penetrates into the SecYEG channel during insertion, contacting most channel transmembrane helices and periplasmic regions.

Substrate Proteins Take Shape at an Improved Bacterial Translocon.