S. M. Theg

Cell-penetrating peptides stimulate protein transport on the Twin-arginine translocation pathway: evidence for a membrane thinning and toroidal pore mechanism

The paper shows membrane thinning stimulates the Tat pathway and membrane strengthening blocks it, supporting a toroidal pore mechanism for protein transport.

A Real-Time Analysis of Protein Transport via the Twin Arginine Translocation Pathway in Response to Different Components of the Protonmotive Force in vivo

This study develops a real-time assay to analyze the energy requirements of the Tat pathway in E. coli, showing that both ΔpH and Δψ contribute to protein transport in vivo.

Functional analysis of the polar amino acid in TatA transmembrane helix

The paper examines the functional role of a polar amino acid in the TatA transmembrane helix of Escherichia coli, finding that while preferred, it is not essential for Tat activity, with hydrophobicity and charge affecting transport efficiency.

Hydrophobic mismatch is a key factor in protein transport on the Tat pathway

This study modifies the transmembrane helix lengths of TatA and TatB in E. coli to assess the role of hydrophobic mismatch in Tat pathway function, finding that 15 residues are optimal for membrane integrity and transport activity.

Chloroplast chaperonin-mediated targeting of a thylakoid membrane protein

The paper shows chloroplast chaperonin Cpn60 captures and releases Plsp1 for thylakoid membrane integration, while cpSecA1 recognizes free Plsp1 for insertion.

Lipid Chaperoning of a Thylakoid Protease Whose Stability is Modified by the Protonmotive Force

The paper investigates how lipid interactions and disulfide bonds affect the stability and activity of Plsp1, a thylakoid membrane protease, under varying pH conditions.

Evaluating the Functional Pore Size of Chloroplast TOC and TIC Protein Translocons

The paper investigates the pore size of chloroplast TOC and TIC translocons and finds they can transport folded proteins like DHFR, suggesting a larger pore size than previously thought.