Characterization of the Consequences of YidC Depletion on the Inner Membrane Proteome of E. coli Using 2D Blue Native/SDS-PAGE

Wickström, David; Wagner, Samuel; Simonsson, Per; Pop, Ovidiu I.; Baars, Louise; Ytterberg, A. Jimmy; Wijk, Klaas J. van; Luirink, Joen; Gier, Jan‐Willem L. de

doi:10.1016/j.jmb.2011.03.068

Cited by 38 publications

(28 citation statements)

References 65 publications

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“…In E. coli, YidC is essential (23); therefore, our analysis of phenotypes in the absence of YidC was performed using a strain in which yidC is under the control of an arabinose-inducible promoter, such that growth in the absence of arabinose leads to depletion of YidC. Consistent with YidC being required for the biogenesis of a minority of cytoplasmic membrane proteins, in cells depleted of YidC, the profile of Triton X-100-soluble membrane proteins, which are enriched for cytoplasmic membrane proteins, was grossly preserved compared to that of cells containing YidC (data not shown), as has been described previously (31).…”

Section: Resultssupporting

confidence: 87%

“…In addition, these findings are consistent with our previous observation that IcsA targeting is independent of FtsZ (2). Together with the observation that the protein composition of the membrane is minimally perturbed following YidC depletion (31), it is likely that the effect of YidC on IcsA localization is mediated by one or a small number of YidC-dependent membrane proteins rather than by a pleiotropic effect.…”

Section: Resultsmentioning

confidence: 99%

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Biogenesis of YidC Cytoplasmic Membrane Substrates Is Required for Positioning of Autotransporter IcsA at Future Poles

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Henderson-Frost

et al. 2014

J Bacteriol

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bLocalization of proteins to specific sites within bacterial cells is often critical to their function. In rod-shaped bacteria, proteins involved in diverse and important cell processes localize to the cell poles. The molecular mechanisms by which these proteins are targeted to the pole, however, are poorly understood. The Shigella autotransporter protein IcsA, which is localized to the pole on the surface of the bacterium, is targeted to the pole in the cytoplasm by a mechanism that is conserved across multiple Gramnegative bacterial species and has thus served as an important and informative model for studying polar localization. We present evidence that in Escherichia coli, the establishment of polar positional information recognized by IcsA requires the activity of the cytoplasmic membrane protein insertase YidC. We show that the role of YidC in IcsA localization is independent of the cell septation and cytokinesis proteins FtsQ and FtsEX. FtsQ is required for polar localization of IcsA and, based on cross-linking studies, is inserted in the vicinity of YidC, but, we find, is not dependent on YidC for membrane insertion. FtsEX is a YidC substrate, but we find that it is not required for polar localization of IcsA. These findings indicate that polar positional information recognized by IcsA depends on one or more membrane proteins that require YidC for proper membrane insertion.

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Section: Resultssupporting

confidence: 87%

Section: Resultsmentioning

confidence: 99%

Biogenesis of YidC Cytoplasmic Membrane Substrates Is Required for Positioning of Autotransporter IcsA at Future Poles

Gray

Henderson-Frost

et al. 2014

J Bacteriol

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“…2C, middle panel). PspA is a peripheral IM-associated stress protein that responds to impaired membrane function (26,52). Although the biological function of PspA is far from clear, it appears to play a role in the maintenance of the PMF upon cell envelope stress.…”

Section: Resultsmentioning

confidence: 99%

Role for Escherichia coli YidD in Membrane Protein Insertion

Lavèn

Klepsch

et al. 2011

J Bacteriol

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YidC has an essential but poorly defined function in membrane protein insertion and folding in bacteria. The yidC gene is located in a gene cluster that is highly conserved in Gram-negative bacteria, the gene order being rpmH, rnpA, yidD, yidC, and trmE. Here, we show that Escherichia coli yidD, which overlaps with rnpA and is only 2 bp upstream of yidC, is expressed and localizes to the inner membrane, probably through an amphipathic helix. Inactivation of yidD had no discernible effect on cell growth and viability. However, compared to control cells, ⌬yidD cells were affected in the insertion and processing of three YidC-dependent inner membrane proteins. Furthermore, in vitro cross-linking showed that YidD is in proximity of a nascent inner membrane protein during its localization in the Sec-YidC translocon, suggesting that YidD might be involved in the insertion process.

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“…Quantitative studies on the total membrane proteome of B. subtilis (Saller et al , 2011 ) and E. coli Wickstrom et al , 2011 ) provide a detailed insight in the effort of the cells to overcome the absence of SpoIIIJ/YqjG and YidC. YidC depletion results in the overexpression of proteins involved in chaperone-induced stress response, such as PspA in E. coli (van der Laan et al , 2003 ) and LiaH in B. subtilis (Jordan et al , 2006 ).…”

Section: Membrane Quality Controlmentioning

confidence: 99%

“…This complex is thought to function in the quality control of membrane proteins in which YidC acts as chaperone and FtsH as protease that degrades misassembled membrane proteins (Ito and Akiyama , 2005 ). Although an increased level of FtsH was detected by proteomic analysis based on two-dimensional gel electrophoresis (Wickstrom et al , 2011 ), proteomic studies using metabolic labeling Saller et al , 2011 ) revealed no alteration of FtsH amount. Instead, HtpX, an FtsH homolog, which is believed to act in quality control (Shimohata et al , 2002 ), was found to be increased in both E. coli and B. subtilis .…”

Section: Membrane Quality Controlmentioning

confidence: 99%

The YidC/Oxa1/Alb3 protein family: common principles and distinct features

Saller

Keyzer

et al. 2012

Biological Chemistry

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The members of the YidC/Oxa1/Alb3 protein family are evolutionary conserved in all three domains of life. They facilitate the insertion of membrane proteins into bacterial, mitochondrial, and thylakoid membranes and have been implicated in membrane protein folding and complex formation. The major classes of substrates are small hydrophobic subunits of large energy-transducing complexes involved in respiration and light capturing. All YidC-like proteins share a conserved membrane region, whereas the N- and C-terminal regions are diverse and fulfill accessory functions in protein targeting.

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Characterization of the Consequences of YidC Depletion on the Inner Membrane Proteome of E. coli Using 2D Blue Native/SDS-PAGE

Cited by 38 publications

References 65 publications

Biogenesis of YidC Cytoplasmic Membrane Substrates Is Required for Positioning of Autotransporter IcsA at Future Poles

Biogenesis of YidC Cytoplasmic Membrane Substrates Is Required for Positioning of Autotransporter IcsA at Future Poles

Role for Escherichia coli YidD in Membrane Protein Insertion

The YidC/Oxa1/Alb3 protein family: common principles and distinct features

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