In vivo membrane topology of Escherichia coli SecA ATPase reveals extensive periplasmic exposure of multiple functionally important domains clustering on one face of SecA. (Q54450403)

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English	In vivo membrane topology of Escherichia coli SecA ATPase reveals extensive periplasmic exposure of multiple functionally important domains clustering on one face of SecA.	scientific article

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

30 May 2018

http://europepmc.org/abstract/MED/17166834

In vivo membrane topology of Escherichia coli SecA ATPase reveals extensive periplasmic exposure of multiple functionally important domains clustering on one face of SecA. (English)

1 reference

Europe PubMed Central

PubMed publication ID

30 May 2018

http://europepmc.org/abstract/MED/17166834

Escherichia coli

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author name string

Lucia B Jilaveanu

1

1 reference

Europe PubMed Central

PubMed publication ID

30 May 2018

http://europepmc.org/abstract/MED/17166834

Donald B Oliver

2

1 reference

Europe PubMed Central

PubMed publication ID

30 May 2018

http://europepmc.org/abstract/MED/17166834

language of work or name

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publication date

13 December 2006

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Europe PubMed Central

PubMed publication ID

30 May 2018

http://europepmc.org/abstract/MED/17166834

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

30 May 2018

http://europepmc.org/abstract/MED/17166834

282

1 reference

Europe PubMed Central

PubMed publication ID

30 May 2018

http://europepmc.org/abstract/MED/17166834

7

1 reference

Europe PubMed Central

PubMed publication ID

30 May 2018

http://europepmc.org/abstract/MED/17166834

4661-4668

1 reference

Europe PubMed Central

PubMed publication ID

30 May 2018

http://europepmc.org/abstract/MED/17166834

The protein-conducting channel SecYEG.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

Structure and function of SecA, the preprotein translocase nanomotor

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

SecB, one small chaperone in the complex milieu of the cell

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

Both an N-terminal 65-kDa domain and a C-terminal 30-kDa domain of SecA cycle into the membrane at SecYEG during translocation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

Crystal structure of Mycobacterium tuberculosis SecA, a preprotein translocating ATPase

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

The molecular chaperone SecB is released from the carboxy-terminus of SecA during initiation of precursor protein translocation.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

Endogenous SecA catalyzes preprotein translocation at SecYEG.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

Selective SecA association with signal sequences in ribosome-bound nascent chains: a potential role for SecA in ribosome targeting to the bacterial membrane.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

SecA protein is exposed to the periplasmic surface of the E. coli inner membrane in its active state.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

Topology of the integral membrane form of Escherichia coli SecA protein reveals multiple periplasmically exposed regions and modulation by ATP binding.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

The oligomeric distribution of SecYEG is altered by SecA and translocation ligands

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

Structure of the E. coli protein-conducting channel bound to a translating ribosome

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

Disulfide bridge formation between SecY and a translocating polypeptide localizes the translocation pore to the center of SecY.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

Protein translocation in the three domains of life: variations on a theme

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

Membrane topology and insertion of membrane proteins: search for topogenic signals

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

Use of T7 RNA polymerase to direct expression of cloned genes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

Dimeric SecA is essential for protein translocation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

Nucleotide sequence of the secA gene and secA(Ts) mutations preventing protein export in Escherichia coli.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

Sequencing reveals similarity of the wild-type div+ gene of Bacillus subtilis to the Escherichia coli secA gene

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

3-(N-Maleimido-propionyl)biocytin: a versatile thiol-specific biotinylating reagent

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

Membrane topology of a cysteine-less mutant of human P-glycoprotein

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

Topology of RbsC, the membrane component of the Escherichia coli ribose transporter

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

Two-stage binding of SecA to the bacterial translocon regulates ribosome-translocon interaction

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

Conformational state of the SecYEG-bound SecA probed by single tryptophan fluorescence spectroscopy

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

SecA is an intrinsic subunit of the Escherichia coli preprotein translocase and exposes its carboxyl terminus to the periplasm.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

SecA, the peripheral subunit of the Escherichia coli precursor protein translocase, is functional as a dimer.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

Covalently dimerized SecA is functional in protein translocation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

SecA dimer cross-linked at its subunit interface is functional for protein translocation

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

Dissociation of the dimeric SecA ATPase during protein translocation across the bacterial membrane

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

Identification of the preprotein binding domain of SecA.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

Demonstration of a specific Escherichia coli SecY-signal peptide interaction

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

Probing the affinity of SecA for signal peptide in different environments

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

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

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

Integration of SecA protein into the Escherichia coli inner membrane is regulated by its amino-terminal ATP-binding domain

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

E. coli mutant pleiotropically defective in the export of secreted proteins

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

Reconstitution of Purified Bacterial Preprotein Translocase in Liposomes

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

Two Independent Mechanisms Down-regulate the Intrinsic SecA ATPase Activity

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M610828200

21 January 2018

Identifiers

10.1074/JBC.M610828200

1 reference

Europe PubMed Central

PubMed publication ID

30 May 2018

http://europepmc.org/abstract/MED/17166834

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

30 May 2018

http://europepmc.org/abstract/MED/17166834

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