Global co-ordination of protein translocation by the SecA IRA1 switch (Q44790621)

6 December 2017

title

Global co-ordination of protein translocation by the SecA IRA1 switch (English)

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6 December 2017

5

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6 December 2017

Eleftheria Vrontou

1

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6 December 2017

Spyridoula Karamanou

series ordinal

2

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6 December 2017

Catherine Baud

series ordinal

3

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6 December 2017

Giorgos Sianidis

series ordinal

4

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6 December 2017

language of work or name

English

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publication date

7 March 2004

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Journal of Biological Chemistry

6 December 2017

published in

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6 December 2017

volume

279

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6 December 2017

issue

21

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6 December 2017

page(s)

22490-22497

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The structural basis of protein targeting and translocation in bacteria.

6 December 2017

cites work

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https://api.crossref.org/works/10.1074%2FJBC.M401008200

Bacterial secretome: the assembly manual and operating instructions (Review).

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M401008200

SecYEG assembles into a tetramer to form the active protein translocation channel

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M401008200

Three-dimensional structure of the bacterial protein-translocation complex SecYEG

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M401008200

The binding cascade of SecB to SecA to SecY/E mediates preprotein targeting to the E. coli plasma membrane

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M401008200

The purified E. coli integral membrane protein SecY/E is sufficient for reconstitution of SecA-dependent precursor protein translocation.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M401008200

SecYEG and SecA Are the Stoichiometric Components of Preprotein Translocase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M401008200

Distinct catalytic roles of the SecYE, SecG and SecDFyajC subunits of preprotein translocase holoenzyme

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M401008200

The SecDFyajC domain of preprotein translocase controls preprotein movement by regulating SecA membrane cycling

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M401008200

The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M401008200

SecA promotes preprotein translocation by undergoing ATP-driven cycles of membrane insertion and deinsertion.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M401008200

SecA membrane cycling at SecYEG is driven by distinct ATP binding and hydrolysis events and is regulated by SecD and SecF.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M401008200

Bacterial preprotein translocase: mechanism and conformational dynamics of a processive enzyme.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M401008200

ΔμH+ and ATP function at different steps of the catalytic cycle of preprotein translocase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M401008200

Cross-talk between catalytic and regulatory elements in a DEAD motor domain is essential for SecA function

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M401008200

Allosteric communication between signal peptides and the SecA protein DEAD motor ATPase domain.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M401008200

Nucleotide control of interdomain interactions in the conformational reaction cycle of SecA

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M401008200

Crystal structure of Mycobacterium tuberculosis SecA, a preprotein translocating ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M401008200

Helicase structure and mechanism

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M401008200

Helicase mechanisms and the coupling of helicases within macromolecular machines. Part I: Structures and properties of isolated helicases

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M401008200

Autogenous translation regulation by Escherichia coli ATPase SecA may be mediated by an intrinsic RNA helicase activity of this protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M401008200

The C terminus of SecA is involved in both lipid binding and SecB binding.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M401008200

Multiple roles for ATP hydrolysis in nucleic acid modifying enzymes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M401008200

Two distinct ATP-binding domains are needed to promote protein export by Escherichia coli SecA ATPase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M401008200

Isolation and analysis of dominant secA mutations in Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M401008200

Lipid and signal peptide-induced conformational changes within the C-domain of Escherichia coli SecA protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M401008200

Functional signal peptides bind a soluble N-terminal fragment of SecA and inhibit its ATPase activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M401008200

Diversity of conformational states and changes within the EF-hand protein superfamily

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M401008200

Stability and solvent accessibility of SecA protein of Escherichia coli

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M401008200

ATP synthase--a marvellous rotary engine of the cell.

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M401008200

A molecular switch in SecA protein couples ATP hydrolysis to protein translocation

21 January 2018

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https://api.crossref.org/works/10.1074%2FJBC.M401008200

21 January 2018

Identifiers

DOI

10.1074/JBC.M401008200

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6 December 2017

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