F(1)F(0) ATP synthase subunit c is targeted by the SRP to YidC in the E. coli inner membrane. (Q54498083)

30 May 2018

title

F(1)F(0) ATP synthase subunit c is targeted by the SRP to YidC in the E. coli inner membrane. (English)

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30 May 2018

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5

Joen Luirink

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author name string

Edwin van Bloois

1

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Gert Jan Haan

2

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Jan-Willem de Gier

3

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Bauke Oudega

4

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Joen Luirink

5

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language of work or name

English

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publication date

1 October 2004

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30 May 2018

published in

FEBS Letters

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volume

576

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issue

1-2

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page(s)

97-100

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Biogenesis of inner membrane proteins in Escherichia coli

cites work

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YidC, a newly defined evolutionarily conserved protein, mediates membrane protein assembly in bacteria

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

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YidC, an assembly site for polytopic Escherichia coli membrane proteins located in immediate proximity to the SecYE translocon and lipids

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Versatility of inner membrane protein biogenesis in Escherichia coli.

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A conserved function of YidC in the biogenesis of respiratory chain complexes.

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Subunit organization and structure in the F0 sector of Escherichia coli F1F0 ATP synthase

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21 January 2018

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21 January 2018

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L23 protein functions as a chaperone docking site on the ribosome

21 January 2018

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FtsH (HflB) is an ATP-dependent protease selectively acting on SecY and some other membrane proteins

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The preferred stoichiometry of c subunits in the rotary motor sector of Escherichia coli ATP synthase is 10.

21 January 2018

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YidC is strictly required for membrane insertion of subunits a and c of the F(1)F(0)ATP synthase and SecE of the SecYEG translocase.

21 January 2018

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

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Differential use of the signal recognition particle translocase targeting pathway for inner membrane protein assembly in Escherichia coli

21 January 2018

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Direct interaction of YidC with the Sec-independent Pf3 coat protein during its membrane protein insertion

21 January 2018

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Basic amino acids in a distinct subset of signal peptides promote interaction with the signal recognition particle

21 January 2018

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The presence of a helix breaker in the hydrophobic core of signal sequences of secretory proteins prevents recognition by the signal-recognition particle in Escherichia coli

21 January 2018

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Functional interaction of chloroplast SRP/FtsY with the ALB3 translocase in thylakoids: substrate not required

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Sec/SRP requirements and energetics of membrane insertion of subunits a, b, and c of the Escherichia coli F1F0 ATP synthase.

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21 January 2018

Identifiers

DOI

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30 May 2018

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30 May 2018