F1F0 ATP synthase subunit c is a substrate of the novel YidC pathway for membrane protein biogenesis

Laan, Martin van der; Bechtluft, Philipp; Kol, Stefan; Nouwen, Nico; Driessen, Arnold J. M.

doi:10.1083/jcb.200402100

Cited by 191 publications

(194 citation statements)

References 47 publications

Supporting

Mentioning

181

Contrasting

Unclassified

Order By: Relevance

“…43). On the other hand, YidC is required to integrate the AtpH ortholog in bacteria, F o c (44), and it has been suggested that many short membrane proteins with C-terminal signal anchor sequences are posttranslationally integrated by the YidC translocon (45). The degree to which ALB3 (the chloroplast YidC ortholog) participates in the posttranslational integration of plastid-encoded proteins remains to be determined.…”

Section: Discussionmentioning

confidence: 99%

Genome-wide analysis of thylakoid-bound ribosomes in maize reveals principles of cotranslational targeting to the thylakoid membrane

Zoschke

Barkan

2015

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

View full text Add to dashboard Cite

Chloroplast genomes encode ∼37 proteins that integrate into the thylakoid membrane. The mechanisms that target these proteins to the membrane are largely unexplored. We used ribosome profiling to provide a comprehensive, high-resolution map of ribosome positions on chloroplast mRNAs in separated membrane and soluble fractions in maize seedlings. The results show that translation invariably initiates off the thylakoid membrane and that ribosomes synthesizing a subset of membrane proteins subsequently become attached to the membrane in a nucleaseresistant fashion. The transition from soluble to membraneattached ribosomes occurs shortly after the first transmembrane segment in the nascent peptide has emerged from the ribosome. Membrane proteins whose translation terminates before emergence of a transmembrane segment are translated in the stroma and targeted to the membrane posttranslationally. These results indicate that the first transmembrane segment generally comprises the signal that links ribosomes to thylakoid membranes for cotranslational integration. The sole exception is cytochrome f, whose cleavable N-terminal cpSecA-dependent signal sequence engages the thylakoid membrane cotranslationally. The distinct behavior of ribosomes synthesizing the inner envelope protein CemA indicates that sorting signals for the thylakoid and envelope membranes are distinguished cotranslationally. In addition, the fractionation behavior of ribosomes in polycistronic transcription units encoding both membrane and soluble proteins adds to the evidence that the removal of upstream ORFs by RNA processing is not typically required for the translation of internal genes in polycistronic chloroplast mRNAs.ribosome profiling | protein targeting | plastid | chloroplast | SecA

show abstract

Section: Discussionmentioning

confidence: 99%

Genome-wide analysis of thylakoid-bound ribosomes in maize reveals principles of cotranslational targeting to the thylakoid membrane

Zoschke

Barkan

2015

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

View full text Add to dashboard Cite

show abstract

“…c-monomers (37). Therefore, it is likely that YidC has an overlapping function with UncI and can complement the UncI deficiency.…”

Section: Discussionmentioning

confidence: 99%

The product of uncI gene in F ₁ F _o -ATP synthase operon plays a chaperone-like role to assist c -ring assembly

Suzuki

Ozaki

Sone³

et al. 2007

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

View full text Add to dashboard Cite

Bacterial operons for F1Fo-ATP synthase typically include an uncI gene that encodes a function-unknown small hydrophobic protein.When we expressed a hybrid F 1Fo (F1 from thermophilic Bacillus PS3 and Na ؉ -translocating Fo from Propionigenium modestum) in Escherchia coli cells, we found that uncI derived from P. modestum was indispensable to produce active enzyme; without uncI, csubunits in F 1Fo existed as monomers but not as functional c11-ring. When uncI was expressed from another plasmid at the same time, active F 1Fo with c11-ring was produced. A plasmid containing only uncI and c-subunit gene produced c 11-ring, but a plasmid containing only c-subunit gene did not. Direct interaction of UncI protein with c-subunits was suggested from copurification of His-tagged UncI protein and c-subunits, both in the state of c 11-ring and c-monomers. Na ؉ induced dissociation of His-tagged UncI protein from c 11-ring but not from c-monomers. These results show that UncI is a chaperone-like protein that assists c 11-ring assembly from c-monomers in the membrane.protein folding ͉ membrane protein ͉ Na ϩ transport

show abstract

“…YidC is homologous to mitochondrial Oxa1p and Alb3p in chloroplasts, both of which are involved in membrane protein biogenesis (30). It is known that integration of many membrane proteins, including not only M13 procoat and Pf3 coat, but also F0c, CyoA, etc., becomes defective upon YidC depletion (31,32). In in vitro experiments, the integrating nascent chains of membrane proteins are efficiently cross-linked to YidC, confirming that YidC interacts and functions together with SecYEG (33,34).…”

Section: Yidcmentioning

confidence: 81%

Glycolipozyme membrane protein integrase (MPIase): recent data

Nishiyama

Shimamoto

2014

Biomolecular Concepts

View full text Add to dashboard Cite

A novel factor for membrane protein integration, from the cytoplasmic membrane of Escherichia coli, named MPIase (membrane protein integrase), has recently been identified and characterized. MPIase was revealed to be essential for the membrane integration of a subset of membrane proteins, despite that such integration reactions have been, thus far, thought to occur spontaneously. The structure determination study revealed that MPIase is a novel glycolipid comprising a glycan chain with three N-acetylated amino sugars connected to diacylglycerol through a pyrophosphate linker. As MPIase catalyzes membrane protein integration, we propose that MPIase is a glycolipozyme on the basis of its enzyme-like function. The glycan chain exhibits a molecular chaperone-like function by directly interacting with substrate membrane proteins. Moreover, MPIase also affects the dimer structure of SecYEG, a translocon, thereby significantly stimulating preprotein translocation. The molecular mechanisms of MPIase functions will be outlined.

show abstract

F1F0 ATP synthase subunit c is a substrate of the novel YidC pathway for membrane protein biogenesis

Cited by 191 publications

References 47 publications

Genome-wide analysis of thylakoid-bound ribosomes in maize reveals principles of cotranslational targeting to the thylakoid membrane

Genome-wide analysis of thylakoid-bound ribosomes in maize reveals principles of cotranslational targeting to the thylakoid membrane

The product of uncI gene in F ₁ F _o -ATP synthase operon plays a chaperone-like role to assist c -ring assembly

Glycolipozyme membrane protein integrase (MPIase): recent data

Contact Info

Product

Resources

About

F1F0 ATP synthase subunit c is a substrate of the novel YidC pathway for membrane protein biogenesis

Cited by 191 publications

References 47 publications

Genome-wide analysis of thylakoid-bound ribosomes in maize reveals principles of cotranslational targeting to the thylakoid membrane

Genome-wide analysis of thylakoid-bound ribosomes in maize reveals principles of cotranslational targeting to the thylakoid membrane

The product of uncI gene in F 1 F o -ATP synthase operon plays a chaperone-like role to assist c -ring assembly

Glycolipozyme membrane protein integrase (MPIase): recent data

Contact Info

Product

Resources

About

The product of uncI gene in F ₁ F _o -ATP synthase operon plays a chaperone-like role to assist c -ring assembly