A unifying mechanism for the biogenesis of membrane proteins co-operatively integrated by the Sec and Tat pathways
- University of Dundee, United Kingdom
- John Innes Centre, United Kingdom
Abstract
The majority of multi-spanning membrane proteins are co-translationally inserted into the bilayer by the Sec pathway. An important subset of membrane proteins have globular, cofactor-containing extracytoplasmic domains requiring the dual action of the co-translational Sec and post-translational Tat pathways for integration. Here, we identify further unexplored families of membrane proteins that are dual Sec-Tat-targeted. We establish that a predicted heme-molybdenum cofactor-containing protein, and a complex polyferredoxin, each require the concerted action of two translocases for their assembly. We determine that the mechanism of handover from Sec to Tat pathway requires the relatively low hydrophobicity of the Tat-dependent transmembrane domain. This, coupled with the presence of C-terminal positive charges, results in abortive insertion of this transmembrane domain by the Sec pathway and its subsequent release at the cytoplasmic side of the membrane. Together, our data points to a simple unifying mechanism governing the assembly of dual targeted membrane proteins.
Article and author information
Author details
Funding
Biotechnology and Biological Sciences Research Council (BB/L000768/1)
- Marion Babot
- Grant Buchanan
Medical Research Council (MR/K500896/1)
- Fiona J Tooke
Biotechnology and Biological Sciences Research Council (BB/J004561/1)
- Govind Chandra
The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.
Copyright
© 2017, Tooke et al.
This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.
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A unifying mechanism for the biogenesis of membrane proteins co-operatively integrated by the Sec and Tat pathways
eLife 6:e26577.
https://doi.org/10.7554/eLife.26577
