Glycosylation limits forward trafficking of the tetraspan membrane protein PMP22.

Peripheral myelin protein 22 (PMP22) folds and trafficks inefficiently, with only 20% of newly expressed protein trafficking to the cell surface. This behavior is exacerbated in many of the mutants associated with Charcot-Marie-Tooth disease, motivating further study. Here we characterized the role of N-glycosylation in limiting PMP22 trafficking.

Continuous Wave Electron Paramagnetic Resonance Spectroscopy Reveals the Structural Topology and Dynamic Properties of Active Pinholin S68 in a Lipid Bilayer.

Pinholin S68 is an essential part of the phage Φ21 lytic protein system to release the virus progeny at the end of the infection cycle. It is known as the simplest natural timing system for its precise control of hole formation in the inner cytoplasmic membrane. Pinholin S68 is a 68 amino acid integral membrane protein consisting of two transmembrane domains (TMDs) called TMD1 and TMD2.

Solid phase synthesis and spectroscopic characterization of the active and inactive forms of bacteriophage S pinholin protein.

The mechanism for the lysis pathway of double-stranded DNA bacteriophages involves a small hole-forming class of membrane proteins, the holins. This study focuses on a poorly characterized class of holins, the pinholin, of which the S protein of phage ϕ21 is the prototype. Here we report the first in vitro synthesis of the wildtype form of the S pinholin, S68, and negative-dominant mutant form, SIRS, both prepared using solid phase peptide synthesis and studied using biophysical techniques.