YfgM Is an Ancillary Subunit of the SecYEG Translocon in Escherichia coli

Götzke, Hansjörg; Palombo, Isolde; Muheim, Claudio; Perrody, Elsa; Genevaux, Pierre; Kudva, Renuka; Müller, Matthias; Daley, Daniel O.

doi:10.1074/jbc.m113.541672

Cited by 51 publications

(61 citation statements)

References 59 publications

(75 reference statements)

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“…Although these putative substrates did not contain any obvious sequence similarities, it is anticipated that their trafficking into the envelope takes place through the SecYEG translocon, as we did not detect any known substrates of the Twin Arginine Translocation (TAT) system (33), or YidC (when independent of SecYEG) (34). This observation is consistent with the observation that YfgM operates at the SecYEG translocon (13).…”

Section: Comparative Proteomic Analyses Of Strains Lacking Yfgm-supporting

confidence: 79%

“…types identified in the ⌬skp and ⌬surA strains (i.e. compromised outer membrane integrity and activation of cell envelope stress responses) are exacerbated when yfgM is deleted (13). It is therefore possible that Skp and SurA compensate for the absence of YfgM and prevent the identification of some potential substrates.…”

Section: Comparative Proteomic Analyses Of Strains Lacking Yfgm-mentioning

confidence: 99%

“…For example, the ⌬skp strain was a complemented double deletion (⌬skp⌬yfgM ϩ pSC-yfgM), and the ⌬skp⌬yfgM strain is the same strain with an empty plasmid (⌬skp⌬yfgM ϩ pSC). In all cases, the expression levels of YfgM were similar to an isogenic parent strain, MC4100 (13). All strains were grown in LB broth supplemented with 50 g/ml kanamycin and 17 g/ml chloramphenicol at 37°C, shaking at 200 rpm to an optical density of OD 600 nm ϳ0.8.…”

Section: Methodsmentioning

confidence: 99%

“…This conclusion is partially based in the fact that YfgM interacts with PpiD and the SecYEG translocon (the guilt-by-association principle; and 5B (11,13)). It is also based on the observation that the role of YfgM partially overlaps with SurA and Skp ( Fig.…”

Section: Comparative Proteomic Analyses Of Strains Lacking Yfgm-mentioning

confidence: 99%

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Identification of Putative Substrates for the Periplasmic Chaperone YfgM in Escherichia coli Using Quantitative Proteomics

Götzke

Muheim

Altelaar

et al. 2015

Molecular & Cellular Proteomics

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How proteins are trafficked, folded, and assembled into functional units in the cell envelope of Gram-negative bacteria is of significant interest. A number of chaperones have been identified, however, the molecular roles of these chaperones are often enigmatic because it has been challenging to assign substrates. Recently we discovered a novel periplasmic chaperone, called YfgM, which associates with PpiD and the SecYEG translocon and operates in a network that contains Skp and SurA. The aim of the study presented here was to identify putative substrates of YfgM. We reasoned that substrates would be incorrectly folded or trafficked when YfgM was absent from the cell, and thus more prone to proteolysis (the loss-of-function rationale). We therefore used a comparative proteomic approach to identify cell envelope proteins that were lower in abundance in a strain lacking yfgM, and strains lacking yfgM together with either skp or surA. Sixteen putative substrates were identified. The list contained nine inner membrane proteins (CusS, EvgS, MalF, OsmC, TdcB, TdcC, WrbA, YfhB, and YtfH) and seven periplasmic proteins (HdeA, HdeB, AnsB, Ggt, MalE, YcgK, and YnjE), but it did not include any lipoproteins or outer membrane proteins. Significantly, AnsB (an asparaginase) and HdeB (a protein involved in the acid stress response), were lower in abundance in all three strains lacking yfgM. For both genes, we ruled out the possibility that they were transcriptionally down-regulated, so it is highly likely that the corresponding proteins are misfolded/mistargeted and turned-over in the absence of YfgM. For HdeB we validated this conclusion in a pulse-chase experiment.

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Section: Comparative Proteomic Analyses Of Strains Lacking Yfgm-supporting

confidence: 79%

Section: Comparative Proteomic Analyses Of Strains Lacking Yfgm-mentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Comparative Proteomic Analyses Of Strains Lacking Yfgm-mentioning

confidence: 99%

See 2 more Smart Citations

Identification of Putative Substrates for the Periplasmic Chaperone YfgM in Escherichia coli Using Quantitative Proteomics

Götzke

Muheim

Altelaar

et al. 2015

Molecular & Cellular Proteomics

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“…Protein BLAST searches indicated that FTS_1680 and FTS_1681 share 28% identity (query cover 93%; E value ϭ 2eϪ15) with YfgM (which contains TPR motifs) of E. coli K-12 and 26% identity (query cover 94%; E value ϭ 6eϪ48) with YfgL of E. coli K-12. Proteins YfgM and YfgL are linked to temperature tolerance (28), and very recently YfgM has been described as a protein involved in the SecYEG system of E. coli (29). To exclude possible polar effects on downstream genes, we evaluated levels of The inFTS_1680 mutant escapes into the host cell cytosol to a lesser extent than the wild-type FSC200 strain.…”

Section: Fig 3 Fts_1680 Is Important For Virulence In Murine Model Ofmentioning

confidence: 99%

Characterization of Tetratricopeptide Repeat-Like Proteins in Francisella tularensis and Identification of a Novel Locus Required for Virulence

et al. 2014

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dFrancisella tularensis is a highly infectious bacterium that causes the potentially lethal disease tularemia. This extremely virulent bacterium is able to replicate in the cytosolic compartments of infected macrophages. To invade macrophages and to cope with their intracellular environment, Francisella requires multiple virulence factors, which are still being identified. Proteins containing tetratricopeptide repeat (TPR)-like domains seem to be promising targets to investigate, since these proteins have been reported to be directly involved in virulence-associated functions of bacterial pathogens. Here, we studied the role of the FTS_0201, FTS_0778, and FTS_1680 genes, which encode putative TPR-like proteins in Francisella tularensis subsp. holarctica FSC200. Mutants defective in protein expression were prepared by TargeTron insertion mutagenesis. We found that the locus FTS_1680 and its ortholog FTT_0166c in the highly virulent Francisella tularensis type A strain SchuS4 are required for proper intracellular replication, full virulence in mice, and heat stress tolerance. Additionally, the FTS_1680-encoded protein was identified as a membrane-associated protein required for full cytopathogenicity in macrophages. Our study thus identifies FTS_1680/ FTT_0166c as a new virulence factor in Francisella tularensis.

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Making a chink in their armor: Current and next-generation antimicrobial strategies against the bacterial cell envelope

Kaderabkova

Mahmood

Furniss

et al. 2023

Advances in Microbial Physiology

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YfgM Is an Ancillary Subunit of the SecYEG Translocon in Escherichia coli

Cited by 51 publications

References 59 publications

Identification of Putative Substrates for the Periplasmic Chaperone YfgM in Escherichia coli Using Quantitative Proteomics

Identification of Putative Substrates for the Periplasmic Chaperone YfgM in Escherichia coli Using Quantitative Proteomics

Characterization of Tetratricopeptide Repeat-Like Proteins in Francisella tularensis and Identification of a Novel Locus Required for Virulence

Making a chink in their armor: Current and next-generation antimicrobial strategies against the bacterial cell envelope

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