YidC Occupies the Lateral Gate of the SecYEG Translocon and Is Sequentially Displaced by a Nascent Membrane Protein

Sachelaru, Ilie; Petriman, Narcis-Adrian; Kudva, Renuka; Kuhn, Patrick; Welte, Thomas; Knapp, Bettina L.; Drepper, Friedel; Warscheid, Bettina; Koch, Hans‐Georg

doi:10.1074/jbc.m112.446583

Cited by 95 publications

(117 citation statements)

References 63 publications

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“…In E. coli, YidC binds to the SecY component of the SecYEG protein-conducting channel, where nascent transmembrane segments laterally escape the translocon (Sachelaru et al, 2013). The critical role of YidC/Alb3 for biogenesis of cyanobacterial and plant thylakoid membranes is well documented (Spence et al, 2004;Göhre et al, 2006).…”

Section: The Yidc Componentmentioning

confidence: 99%

A Cyanobacterial Chlorophyll Synthase-HliD Complex Associates with the Ycf39 Protein and the YidC/Alb3 Insertase

et al. 2014

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Macromolecular membrane assemblies of chlorophyll-protein complexes efficiently harvest and trap light energy for photosynthesis. To investigate the delivery of chlorophylls to the newly synthesized photosystem apoproteins, a terminal enzyme of chlorophyll biosynthesis, chlorophyll synthase (ChlG), was tagged in the cyanobacterium Synechocystis PCC 6803 (Synechocystis) and used as bait in pull-down experiments. We retrieved an enzymatically active complex comprising ChlG and the high-light-inducible protein HliD, which associates with the Ycf39 protein, a putative assembly factor for photosystem II, and with the YidC/Alb3 insertase. 2D electrophoresis and immunoblotting also provided evidence for the presence of SecY and ribosome subunits. The isolated complex contained chlorophyll, chlorophyllide, and carotenoid pigments. Deletion of hliD elevated the level of the ChlG substrate, chlorophyllide, more than 6-fold; HliD is apparently required for assembly of FLAGChlG into larger complexes with other proteins such as Ycf39. These data reveal a link between chlorophyll biosynthesis and the Sec/YidC-dependent cotranslational insertion of nascent photosystem polypeptides into membranes. We expect that this close physical linkage coordinates the arrival of pigments and nascent apoproteins to produce photosynthetic pigmentprotein complexes with minimal risk of accumulating phototoxic unbound chlorophylls.

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Section: The Yidc Componentmentioning

confidence: 99%

A Cyanobacterial Chlorophyll Synthase-HliD Complex Associates with the Ycf39 Protein and the YidC/Alb3 Insertase

et al. 2014

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“…In the SecYEG-mediated co-translational pathway, YidC is suggested to localize in the vicinity of the lateral gate of SecY to facilitate the release of the TMSs from the SecYEG channel into the lipids bilayers and to chaperone the folding and/or assembly (44,48). To further examine whether YidC⌬8 is still functional in the SecYEG-YidC insertion pathway, the membrane insertion of NuoK was explored.…”

Section: The Cytoplasmic Loop C2 and The C Terminus Of Yidc Are Requimentioning

confidence: 99%

Role of the Cytosolic Loop C2 and the C Terminus of YidC in Ribosome Binding and Insertion Activity

Geng

Kedrov

Caumanns

et al. 2015

Journal of Biological Chemistry

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“…Samples were subsequently analyzed by Western blotting using a-TrxA antibodies. Cross-linked products of positions, R146 and 160, migrated in two distinct species, which is a common phenomenon of pBpa cross-linking (25,31,38) and probably reflects different threedimensional structures.…”

Section: Discussionmentioning

confidence: 99%

“…Furthermore, both cross-linked products migrated as a double band; a weaker band migrating at *50 kDa, and a stronger band migrating at *55 kDa. Position-dependent mobility of pBpa cross-linked products on SDS-PAGE is frequently observed (25,31,38) and probably the result of differences in the three-dimensional structures of the cross-linking products. We also noticed less TrxA copurifying with YchF that had pBpa inserted into positions 140 and 160, which could indicate that pBpa insertion at these residues reduces the YchF-TrxA interaction.…”

Section: Ychf Interacts With Thioredoxin 1 In Vivomentioning

confidence: 99%

“…Lanes of an SDS gel of purified samples were cut into equal slices and subjected to in-gel digestion using trypsin, followed by nano-UHPLC/MS analysis essentially as described (38). The LTQ-FT-Ultra (Thermo Fisher Scientific) was operated with settings as described (33), except that survey full MS spectra were collected at a resolution of 25,000 with an automatic gain control target value of 2 · 10 6 ions.…”

Section: Protein Identification and Quantification By Mass Spectrometrymentioning

confidence: 99%

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Redox Activation of the Universally Conserved ATPase YchF by Thioredoxin 1

Hannemann

Suppanz

et al. 2016

Antioxidants & Redox Signaling

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Aims: YchF/Ola1 are unconventional members of the universally conserved GTPase family because they preferentially hydrolyze ATP rather than GTP. These ATPases have been associated with various cellular processes and pathologies, including DNA repair, tumorigenesis, and apoptosis. In particular, a possible role in regulating the oxidative stress response has been suggested for both bacterial and human YchF/Ola1. In this study, we analyzed how YchF responds to oxidative stress and how it potentially regulates the antioxidant response. Results: Our data identify a redox-regulated monomer-dimer equilibrium of YchF as a key event in the functional cycle of YchF. Upon oxidative stress, the oxidation of a conserved and surface-exposed cysteine residue promotes YchF dimerization, which is accompanied by inhibition of the ATPase activity. No dimers were observed in a YchF mutant lacking this cysteine. In vitro, the YchF dimer is dissociated by thioredoxin 1 (TrxA) and this stimulates the ATPase activity. The physiological significance of the YchF-thioredoxin 1 interaction was demonstrated by in vivo cross-linking, which validated this interaction in living cells. This approach also revealed that both the ATPase domain and the helical domain of YchF are in contact with TrxA. Innovation: YchF/Ola1 are the first redox-regulated members of the universally conserved GTPase family and are inactivated by oxidation of a conserved cysteine residue within the nucleotide-binding motif. Conclusion: Our data provide novel insights into the regulation of the so far ill-defined YchF/Ola1 family of proteins and stipulate their role as negative regulators of the oxidative stress response. Antioxid. Redox Signal. 24, 141-156.

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YidC Occupies the Lateral Gate of the SecYEG Translocon and Is Sequentially Displaced by a Nascent Membrane Protein

Cited by 95 publications

References 63 publications

A Cyanobacterial Chlorophyll Synthase-HliD Complex Associates with the Ycf39 Protein and the YidC/Alb3 Insertase

A Cyanobacterial Chlorophyll Synthase-HliD Complex Associates with the Ycf39 Protein and the YidC/Alb3 Insertase

Role of the Cytosolic Loop C2 and the C Terminus of YidC in Ribosome Binding and Insertion Activity

Redox Activation of the Universally Conserved ATPase YchF by Thioredoxin 1

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