Structure and function of the TAM, a nanomachine responsible for the assembly of complex outer membrane proteins

Research output: Contribution to conferencePoster

Abstract

Rapid remodelling of the outer membrane proteome is essential for bacterial survival under fluctuating environmental conditions. We have
found that during host-pathogen interactions, one of the important determinants for successful bacteria is the translocation and assembly
module (TAM), which ensures the rapid deployment of a range of virulence factors. Using a functional assay, we have found that the folding
rates of complex outer membrane proteins are inhibitively slower in the absence of the TAM.
The TAM itself is a membrane-spanning processing centre connecting the outer membrane to the inner membrane through the interaction of
TamA and TamB. TamA has structural homology to the central component of the BAM complex, BamA, which is involved generally in outer
membrane protein biogenesis. Using our assay, we have observed a dynamic interplay between these two nanomachines and found that when
the TAM is absent, the BAM complex can facilitate assembly of complex proteins, albeit with low efficiency. By swapping the conserved domains
of BamA and TamA, we observed that while the N-terminal POTRA domains were important for partner-protein interactions, the subtle
differences in the transmembrane beta-barrel were required for substrate specificity.
Original languageEnglish
Publication statusPublished - 6 Feb 2018
EventLorne Conference on Protein Structure and Function - Lorne Cumberland, 150 Mountjoy Parade, Lorne, Australia
Duration: 4 Feb 20188 Feb 2018
Conference number: 43rd
http://www.lorneproteins.org/past-meetings/past-conference-proceedings/

Conference

ConferenceLorne Conference on Protein Structure and Function
CountryAustralia
CityLorne
Period4/02/188/02/18
Internet address

Cite this

Stubenrauch, C. J. (2018). Structure and function of the TAM, a nanomachine responsible for the assembly of complex outer membrane proteins. Poster session presented at Lorne Conference on Protein Structure and Function, Lorne, Australia.