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Role for Escherichia coli YidD in membrane protein insertion.

ABSTRACT: 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.

SUBMITTER: Yu Z

PROVIDER: S-EPMC3187451 | biostudies-literature | 2011 Oct

REPOSITORIES: biostudies-literature

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Role for Escherichia coli YidD in membrane protein insertion.

Yu Zhong Z Lavèn Mariëlle M Klepsch Mirjam M de Gier Jan-Willem JW Bitter Wilbert W van Ulsen Peter P Luirink Joen J

Journal of bacteriology 20110729 19

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 ...[more]

PMID: 21803992

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Project description:The FasD protein is essential for the biogenesis of 987P fimbriae of Escherichia coli. In this study, subcellular fractionation was used to demonstrate that FasD is an outer membrane protein. In addition, the accessibility of FasD to proteases established the presence of surface-exposed FasD domains on both sides of the outer membrane. The fasD gene was sequenced, and the deduced amino acid sequence was shown to share homologous domains with a family of outer membrane proteins from various fimbrial systems. Similar to porins, fimbrial outer membrane proteins are relatively polar, lack typical hydrophobic membrane-spanning domains, and posses secondary structures predicted to be rich in turns and amphipathic beta-sheets. On the basis of the experimental data and structural predictions, FasD is postulated to consist essentially of surface-exposed turns and loops and membrane-spanning interacting amphipathic beta-strands. In an attempt to test this prediction, the fasD gene was submitted to random in-frame linker insertion mutagenesis. Preliminary experiments demonstrated that it was possible to produce fasD mutants, whose products remain functional for fimbrial export and assembly. Subsequently, 11 fasD alleles, containing linker inserts encoding beta-turn-inducing residues, were shown to express functional proteins. The insertion sites were designated permissive sites. The inserts used are expected to be least detrimental to the function of FasD when they are inserted into surface-exposed domains not directly involved in fimbrial export. In contrast, FasD is not expected to accommodate such residues in its amphipathic beta-strands without being destabilized in the membrane and losing function. All permissive sites were sequenced and shown to be located in or one residue away from predicted turns. In contrast, 5 of 10 sequenced nonpermissive sites were mapped to predicted amphipathic beta-strands. These results are consistent with the structural predictions for FasD.

Dataset Information

Role for Escherichia coli YidD in membrane protein insertion.

Publications

Role for Escherichia coli YidD in membrane protein insertion.

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