The hydrophobic core of twin-arginine signal sequences orchestrates specific binding to Tat-pathway related chaperones.
Redox enzyme maturation proteins (REMPs) bind pre-proteins destined for translocation across the bacterial cytoplasmic membrane via the twin-arginine translocation system and enable the enzymatic incorporation of complex cofactors. Most REMPs recognize one specific pre-protein. The recognition site...
Main Authors: | Anitha Shanmugham, Adil Bakayan, Petra Völler, Joost Grosveld, Holger Lill, Yves J M Bollen |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2012-01-01
|
Series: | PLoS ONE |
Online Access: | http://europepmc.org/articles/PMC3316669?pdf=render |
Similar Items
-
Structure of the TatC core of the twin-arginine protein transport system.
by: Rollauer, SE, et al.
Published: (2012) -
Structure of the TatC core of the twin-arginine protein transport system
by: Rollauer, SE, et al.
Published: (2012) -
Twin-arginine translocase component TatB performs folding quality control via a chaperone-like activity
by: May N. Taw, et al.
Published: (2022-09-01) -
The twin-arginine translocation (Tat) protein export pathway
by: Palmer, T, et al.
Published: (2012) -
Genetic evidence for a TatC dimer at the core of the Escherichia coli twin arginine (Tat) protein translocase.
by: Maldonado, B, et al.
Published: (2011)