Protein translocation across the inner membrane of Gram-negative bacteria: the Sec and Tat dependent protein transport pathways

Kudva, Renuka; Denks, Kärt; Kuhn, Patrick; Vogt, Andreas; Müller, Matthias; Koch, Hans‐Georg

doi:10.1016/j.resmic.2013.03.016

Cited by 151 publications

(154 citation statements)

References 391 publications

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“…This folding is necessary for hydrolysis of peptide bonds near or in the membrane at the trans-side (2), although premature folding would lead to incorrect insertion from the cis-side. In bacteria, this problem is prevented by co-translational transport by the SRP pathway, which initiates translocation of unfolded polypeptide chain, whereas it is still attached to ribosomes (66,67). This system also exists in chloroplasts, as demonstrated by co-translational insertion of LepB into isolated thylakoids (68).…”

Section: Discussionmentioning

confidence: 99%

“…Antisera Used for Immunoblotting and Antibody Inhibition Assay-Antisera used for immunoblotting include those against a His tag (His probe, H-15; Santa Cruz Biotechnology), Plsp1 276 -291 (20), human Hsp60 (SPA807; Enzo Life Sciences, Farmingdale, NY), and pea Hsp70 (66). For the antibody inhibition assay, antisera against pea translocon components (Alb3, cpSecY1, and Hcf106) were used (30).…”

Section: Preparation Of Recombinant Proteins-production Of His 6 -Tagmentioning

confidence: 99%

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Chaperone-assisted Post-translational Transport of Plastidic Type I Signal Peptidase 1

Endow

Singhal

Fernandez

et al. 2015

Journal of Biological Chemistry

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Background:In bacteria, type I signal peptidase is targeted to the membrane co-translationally. Results: Plastidic type I signal peptidase 1 (Plsp1) could insert into the membrane in an incorrect orientation, which was prevented by a stroma chaperone and the cpSec1 machine. Conclusion: Correct membrane insertion of Plsp1 is ensured by stromal components.Significance: The results demonstrate an adaptive mechanism of protein transport during organelle evolution.

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Section: Discussionmentioning

confidence: 99%

Section: Preparation Of Recombinant Proteins-production Of His 6 -Tagmentioning

confidence: 99%

Chaperone-assisted Post-translational Transport of Plastidic Type I Signal Peptidase 1

Endow

Singhal

Fernandez

et al. 2015

Journal of Biological Chemistry

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“…Many integral membrane proteins (IMPs) are synthesized by membrane-bound ribosomes and are transferred directly from the ribosomes into the membrane by protein translocases or insertases (du Plessis et al, 2011;Facey and Kuhn, 2010;Johnson, 2009;Kudva et al, 2013;Neugebauer et al, 2012;Rapoport, 2007;Zimmermann et al, 2011). The targeting of ribosomes translating IMPs to the translocases or insertases is proposed to be mediated mainly by the evolutionarily conserved signal recognition particle (SRP) system composed of the SRP (Ffh protein and 4.5S RNA in Escherichia coli) and its receptor (FtsY in E. coli) (Walter and Johnson, 1994).…”

Section: Introductionmentioning

confidence: 99%

Co-translational membrane association of the Escherichia coli SRP receptor

Bercovich-Kinori

Bibi

2015

Journal of Cell Science

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The signal recognition particle (SRP) receptor is a major player in the pathway of membrane protein biogenesis in all organisms. The receptor functions as a membrane-bound entity but very little is known about its targeting to the membrane. Here, we demonstrate in vivo that the Escherichia coli SRP receptor targets the membrane co-translationally. This requires emergence from the ribosome of the four-helix-long N-domain of the receptor, of which only helices 2-4 are required for co-translational membrane attachment. The results also suggest that the targeting might be regulated co-translationally. Taken together, our in vivo studies shed light on the biogenesis of the SRP receptor and its hypothetical role in targeting ribosomes to the E. coli membrane.

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“…As DmsC is a polytopic integral membrane protein with eight transmembrane segments, it is likely translocated and inserted into the membrane by one of the two known pathways in bacteria as opposed to spontaneous insertion (99,100). Truncation studies have demonstrated that the C-terminus of DmsB is indispensable for anchoring to DmsC, suggesting that the direct docking of DmsAB to DmsC is likely solely through interactions with DmsB (42) in agreement with the overall structural architecture of CISM systems.…”

Section: Stage 15: Anchoring To Dmscmentioning

confidence: 76%

Assembly pathway of a bacterial complex iron sulfur molybdoenzyme

Cherak

Turner

2017

Biomolecular Concepts

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Protein folding and assembly into macromolecule complexes within the living cell are complex processes requiring intimate coordination. The biogenesis of complex iron sulfur molybdoenzymes (CISM) requires use of a system specific chaperone -a redox enzyme maturation protein (REMP) -to help mediate final folding and assembly. The CISM dimethyl sulfoxide (DMSO) reductase is a bacterial oxidoreductase that utilizes DMSO as a final electron acceptor for anaerobic respiration. The REMP DmsD strongly interacts with DMSO reductase to facilitate folding, cofactor-insertion, subunit assembly and targeting of the multi-subunit enzyme prior to membrane translocation and final assembly and maturation into a bioenergetic catalytic unit. In this article, we discuss the biogenesis of DMSO reductase as an example of the participant network for bacterial CISM maturation pathways.

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Protein translocation across the inner membrane of Gram-negative bacteria: the Sec and Tat dependent protein transport pathways

Cited by 151 publications

References 391 publications

Chaperone-assisted Post-translational Transport of Plastidic Type I Signal Peptidase 1

Chaperone-assisted Post-translational Transport of Plastidic Type I Signal Peptidase 1

Co-translational membrane association of the Escherichia coli SRP receptor

Assembly pathway of a bacterial complex iron sulfur molybdoenzyme

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