Concerted folding and binding of a flexible colicin domain to its periplasmic receptor TolA.

Compared with folded structures, natively unfolded protein domains are over-represented in protein-protein and protein-DNA interactions. Such domains are common features of all colicins and are required for their translocation across the outer membrane of the target Escherichia coli cell. All of these domains bind to at least one periplasmic protein of the Tol or Ton family.

Mutations of penicillin acylase residue B71 extend substrate specificity by decreasing steric constraints for substrate binding.

Two mutant forms of penicillin acylase from Escherichia coli strains, selected using directed evolution for the ability to use glutaryl-L-leucine for growth [Forney, Wong and Ferber (1989) Appl. Environ. Microbiol.

Regulation of phosphatidic acid phosphohydrolase 1 by fatty acids.

In the starved state and during metabolic stress, free fatty acids (FFA) are the principal hepatic energy supply, undergoing beta-oxidation. Accordingly, it appears paradoxical that FFA have been reported to increase the liver's esterification capacity by translocating the rate-limiting enzyme phosphatidic acid phosphohydrolase (PAP-1) from the cytosol to the endoplasmic reticulum. We have therefore investigated the regulation of rat liver PAP-1.