YidC, the Escherichia coli homologue of mitochondrial Oxa1p, is a component of the Sec translocase

Scotti, Pier A.; Urbanus, Malene L.; Brunner, Josef; Gier, Jan‐Willem L. de; Heijne, Gunnar von; Does, Chris van der; Driessen, Arnold J.M.; Oudega, Bauke; Luirink, Joen

doi:10.1093/emboj/19.4.542

Cited by 350 publications

(440 citation statements)

References 41 publications

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“…On the other hand, initial membrane insertion of nascent FtsQ does not depend on SecA, although these translation-arrested nascent chains can be cross-linked to SecA (4,11). Because the translation lysate contains wild-type levels of SecA, SecYEG proteoliposomes were tested with a lysate that was immunodepleted from SecA.…”

Section: Fig 2 the Pmf Is Required For Membrane Insertion Of Ftsqmentioning

confidence: 99%

SecYEG Proteoliposomes Catalyze the Δϕ-Dependent Membrane Insertion of FtsQ

Laan

Nouwen

Driessen

2004

Journal of Biological Chemistry

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In Escherichia coli, the insertion of most inner membrane proteins is mediated by the Sec translocase. Ribosome-bound nascent chains of Sec-dependent inner membrane proteins are targeted to the SecYEG complex via the signal recognition particle pathway. We now demonstrate that the signal recognition particledependent co-translational membrane targeting and membrane insertion of FtsQ can be reconstituted with proteoliposomes containing purified SecYEG. SecA and a transmembrane electrical potential are essential for the translocation of the large periplasmic domain of FtsQ, whereas co-reconstituted YidC has an inhibitory effect. These data demonstrate that membrane protein insertion can be reconstituted with a minimal set of purified Sec components.

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Section: Fig 2 the Pmf Is Required For Membrane Insertion Of Ftsqmentioning

confidence: 99%

SecYEG Proteoliposomes Catalyze the Δϕ-Dependent Membrane Insertion of FtsQ

Laan

Nouwen

Driessen

2004

Journal of Biological Chemistry

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“…Both proteins have been conserved and are found in mitochondria of fungi, plants, and animals (Preuss et al, 2005). These proteins are related in sequence to the Escherichia coli YidC protein that is involved in membrane protein assembly in bacteria (Samuelson et al, 2000;Scotti et al, 2000). Depending on the substrate protein that is integrated into the membrane, YidC acts either as a separate unit or in connection with the Sec-YEG translocon (Samuelson et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

One of Two Alb3 Proteins Is Essential for the Assembly of the Photosystems and for Cell Survival in Chlamydomonas

et al. 2006

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Proteins of the YidC/Oxa1p/ALB3 family play an important role in inserting proteins into membranes of mitochondria, bacteria, and chloroplasts. In Chlamydomonas reinhardtii, one member of this family, Albino3.1 (Alb3.1), was previously shown to be mainly involved in the assembly of the light-harvesting complex. Here, we show that a second member, Alb3.2, is located in the thylakoid membrane, where it is associated with large molecular weight complexes. Coimmunoprecipitation experiments indicate that Alb3.2 interacts with Alb3.1 and the reaction center polypeptides of photosystem I and II as well as with VIPP1, which is involved in thylakoid formation. Moreover, depletion of Alb3.2 by RNA interference to 25 to 40% of wild-type levels leads to a reduction in photosystems I and II, indicating that the level of Alb3.2 is limiting for the assembly and/or maintenance of these complexes in the thylakoid membrane. Although the levels of several photosynthetic proteins are reduced under these conditions, other proteins are overproduced, such as VIPP1 and the chloroplast chaperone pair Hsp70/ Cdj2. These changes are accompanied by a large increase in vacuolar size and, after a prolonged period, by cell death. We conclude that Alb3.2 is required directly or indirectly, through its impact on thylakoid protein biogenesis, for cell survival.

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“…Truncated mRNA was prepared as described (19). In vitro translation was carried out in the E. coli cell-and membrane-free S-135 extract as described (16).…”

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confidence: 99%

SecB is a bona fide generalized chaperone in Escherichia coli

Ullers

Luirink

Harms

et al. 2004

Proc. Natl. Acad. Sci. U.S.A.

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108

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It is known that the DnaK and Trigger Factor (TF) chaperones cooperate in the folding of newly synthesized cytosolic proteins in Escherichia coli. We recently showed that despite a very narrow temperature range of growth and high levels of aggregated cytosolic proteins, E. coli can tolerate deletion of both chaperones, suggesting that other chaperones might be involved in this process. Here, we show that the secretion-dedicated chaperone SecB efficiently suppresses both the temperature sensitivity and the aggregation-prone phenotypes of a strain lacking both TF and DnaK. SecB suppression is independent of a productive interaction with the SecA subunit of the translocon. Furthermore, in vitro cross-linking experiments demonstrate that SecB can interact both co-and posttranslationally with short nascent chains of both secretory and cytosolic proteins. Finally, we show that such cotranslational substrate recognition by SecB is greatly suppressed in the presence of ribosome-bound TF, but not by DnaK. Taken together, our data demonstrate that SecB acts as a bona fide generalized chaperone.

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YidC, the Escherichia coli homologue of mitochondrial Oxa1p, is a component of the Sec translocase

Cited by 350 publications

References 41 publications

SecYEG Proteoliposomes Catalyze the Δϕ-Dependent Membrane Insertion of FtsQ

SecYEG Proteoliposomes Catalyze the Δϕ-Dependent Membrane Insertion of FtsQ

One of Two Alb3 Proteins Is Essential for the Assembly of the Photosystems and for Cell Survival in Chlamydomonas

SecB is a bona fide generalized chaperone in Escherichia coli

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