A unifying mechanism for the biogenesis of membrane proteins co-operatively integrated by the Sec and Tat pathways

ELife
Fiona J TookeTracy Palmer

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.

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Citations

Jan 24, 2020·Molecular Microbiology·Tracy Palmer, Phillip J Stansfeld
Apr 18, 2018·Antibiotics·Sonia Gullón, Rafael P Mellado
May 4, 2021·Frontiers in Molecular Biosciences·Julia OswaldHans-Georg Koch

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Methods Mentioned

BETA
dissection
PCR
Protein Assay

Software Mentioned

Jalview
TMHMM
TATFind
Boxshade
ImageJ
SCAMPI2
ClustalW
TOPCONS
OPTIMIZER
Gimp

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