Chapter 4 : The Conserved Role of YidC in Membrane Protein Biogenesis

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The Conserved Role of YidC in Membrane Protein Biogenesis, Page 1 of 2

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Membrane proteins constitute between 20–30% of the cellular proteome ( ) and perform critical functions like signal transduction, molecular transport, and cell adhesion. The molecular machineries that catalyze their targeting, insertion, and assembly in the different cellular and subcellular membranes are remarkably conserved. The Sec translocon is responsible for moving the majority of the proteins across/into the bacterial, archaeal, thylakoidal, and endoplasmic reticulum (ER) membranes in an unfolded state ( ). In bacteria, it is proposed to form a holocomplex composed of the heterotrimeric protein channel SecYEG and the accessory elements SecDFYajC, SecA ATPase, and YidC ( ).

Citation: Shanmugam S, Dalbey R. 2019. The Conserved Role of YidC in Membrane Protein Biogenesis, p 43-51. In Sandkvist M, Cascales E, Christie P (ed), Protein Secretion in Bacteria. ASM Press, Washington, DC. doi: 10.1128/microbiolspec.PSIB-0014-2018
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Figure 1

YidC family of proteins. (Top) Structural homology in the YidC/Alb3/Oxa1 family, shown by highlighting the conserved TMs in green (TM1), red (TM2), cyan (TM3), purple (TM4), and yellow (TM5). The YidC structure is adapted from the crystal structure solved in (PDB code 3WO7); Alb3 and Oxa1 structures are three-dimensional (3D) computational models made using SWISS-MODEL workspace as described in reference . (Bottom) Newly identified members of the Oxa1 superfamily, with highlighting of the conserved three TM segments in green (TM1), red (TM2), and yellow (TM3). The archaeal DUF106 structure is adapted from the crystal structure solved in (PDB code 5C8J). Yeast Get1, human TMCO1, and human EMC3 structures are evolutionary covariance-based 3D models adapted from those described in references and . The cytoplasmic regions of these models were modified as described in reference .

Citation: Shanmugam S, Dalbey R. 2019. The Conserved Role of YidC in Membrane Protein Biogenesis, p 43-51. In Sandkvist M, Cascales E, Christie P (ed), Protein Secretion in Bacteria. ASM Press, Washington, DC. doi: 10.1128/microbiolspec.PSIB-0014-2018
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Figure 2

Model of YidC-mediated membrane insertion of Pf3 coat protein. This figure is adapted from a review by Kiefer and Kuhn ( ). Binding of Pf3 coat protein to YidC. Pf3 TM segment interacts with the cytoplasmic part of the greasy slide, and the N-terminal tail of Pf3 (blue) enters the hydrophilic cavity of YidC possessing the conserved Arg residue (red). Pf3 coat TM segment inserts across the YidC greasy slide formed by TM3 and TM5 (purple) and release of the N-tail into the periplasmic space. Release of Pf3 into the bilayer.

Citation: Shanmugam S, Dalbey R. 2019. The Conserved Role of YidC in Membrane Protein Biogenesis, p 43-51. In Sandkvist M, Cascales E, Christie P (ed), Protein Secretion in Bacteria. ASM Press, Washington, DC. doi: 10.1128/microbiolspec.PSIB-0014-2018
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Figure 3

Model of the YidC-Sec insertion pathway. The SRP-bound substrate is cotranslationally targeted to the Sec holotranslocon (SecDFYajC [not represented]) via the membrane-associated SRP receptor FtsY. The substrate amino-terminal TM segment inserts at the interface of SecYEG and YidC and the second TM segment initiates C-terminal translocation. The model substrate shown here, Fa, is inserted into the bilayer.

Citation: Shanmugam S, Dalbey R. 2019. The Conserved Role of YidC in Membrane Protein Biogenesis, p 43-51. In Sandkvist M, Cascales E, Christie P (ed), Protein Secretion in Bacteria. ASM Press, Washington, DC. doi: 10.1128/microbiolspec.PSIB-0014-2018
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