We describe the identification of two Escherichia coli genes required for the export of
cofactor‐containing periplasmic proteins, synthesized with signal peptides containing a twin …

The chemical changes which occur during the process of carious destruction of enamel are
complex due to a number of factors. First, substituted hydroxyapatite, the main component of …

Proteins are transported across the bacterial plasma membrane and the chloroplast thylakoid
membrane by means of protein translocases that recognize N-terminal targeting signals in …

Objectives: The purpose of this study was to evaluate the clinical plaque disclosing agent
erythrosine as a photosensitizer in the photodynamic killing of the oral bacterium …

The hydroxyapatite crystals of mature enamel are unusually large, uniform and regularly
disposed within the tissue, implying that their development is a highly controlled process. The …

The twin‐arginine translocation (Tat) system targets cofactor‐containing proteins across the
Escherichia coli cytoplasmic membrane via distinct signal peptides bearing a twin‐arginine …

In Escherichia coli, a subset of periplasmic proteins is exported via the twin-arginine translocation
(Tat) pathway. In the present study, we have purified the Tat complex from E. coli, and …

Using a var2-2 mutant ofArabidopsis thaliana, which lacks a homologue of the zinc-metalloprotease,
FtsH, we demonstrate that this protease is required for the efficient turnover of the …

The albino3 (alb3) mutant of Arabidopsis forms white or light yellow cotyledons and leaves
and when germinated on soil does not survive beyond the seedling stage. The chloroplasts …

The Escherichia coli Tat system mediates Sec-independent export of protein precursors
bearing twin arginine signal peptides. Genes known to be involved in this process include tatA, …