Related Experiment Video
Updated: Mar 19, 2026

Transmembrane Domain Oligomerization Propensity determined by ToxR Assay
Published on: May 26, 2011
Distinct Interaction of TmrB Protein with Membranes in Bacillus subtilis and Escherichia coli
Y Noda1, K Yoda1, M Yamasaki1
1a Department of Agricultural Chemistry , The University of Tokyo , Bunkyo-ku, Tokyo 113 , Japan.
Abstract:
TmrB protein, which endows Bacillus subtilis with tunicamycin resistance, was found to bind more tightly to the membrane in B. subtilis than in E. coli. Although only the C-terminal amphiphilic a-helix was responsible for membrane-TmrB interaction in E. coli, there should be other binding factor(s) in the original strain, B. subtilis.
Related Concept Videos
Bacterial Translocation and Protein Secretion
Tail-anchoring of Proteins in the ER Membrane
Insertion of Single-pass Transmembrane Proteins in the RER
Integral transmembrane proteins possess transmembrane and extra membrane domains. The transmembrane domains are primarily made of 20-25 hydrophobic amino acids arranged in a helical secondary confirmation. These...
Cotranslational Protein Translocation
Sec61 channel partners for cotranslational translocation
During cotranslational translocation, the Sec61 channel partners with the signal recognition particle (SRP), the signal recognition particle receptor (SR), and the ribosomes to transport the nascent polypeptide chain...
Coordination of Gene Expression Processes in Bacteria
Multi-pass Transmembrane Proteins and β-barrels
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...

