Covalently dimerized SecA is functional in protein translocation (Q46663736)

24 December 2017

title

Covalently dimerized SecA is functional in protein translocation (English)

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5

Ben de Kruijff

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Nico Nouwen

6

object named as

Nico Nouwen

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author name string

Jeanine de Keyzer

1

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Eli O van der Sluis

2

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Robin E J Spelbrink

3

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Niels Nijstad

4

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Chris van der Does

7

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Arnold J M Driessen

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language of work or name

English

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publication date

22 August 2005

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Journal of Biological Chemistry

published in

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volume

280

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issue

42

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page(s)

35255-35260

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SecA protein is required for secretory protein translocation into E. coli membrane vesicles.

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506157200

The protein-conducting channel SecYEG.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506157200

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.M506157200

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.M506157200

SecA, an essential component of the secretory machinery of Escherichia coli, exists as homodimer.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506157200

Complex behavior in solution of homodimeric SecA.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506157200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506157200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506157200

Asymmetric binding between SecA and SecB two symmetric proteins: implications for function in export.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506157200

Structural determinants of SecB recognition by SecA in bacterial protein translocation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506157200

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.M506157200

A large conformational change of the translocation ATPase SecA

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506157200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506157200

Phospholipid-induced monomerization and signal-peptide-induced oligomerization of SecA.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506157200

Nucleotide binding induces changes in the oligomeric state and conformation of Sec A in a lipid environment: a small-angle neutron-scattering study

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506157200

The bacterial protein-translocation complex: SecYEG dimers associate with one or two SecA molecules

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506157200

Binding, activation and dissociation of the dimeric SecA ATPase at the dimeric SecYEG translocase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506157200

The bacterial ATPase SecA functions as a monomer in protein translocation.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506157200

Dimeric SecA is essential for protein translocation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506157200

Kinetic analysis of the translocation of fluorescent precursor proteins into Escherichia coli membrane vesicles.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506157200

Direct demonstration of ATP-dependent release of SecA from a translocating preprotein by surface plasmon resonance.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506157200

Detection and identification of stable oligomeric protein complexes in Escherichi coli inner membranes: a proteomics approach.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506157200

Zinc stabilizes the SecB binding site of SecA.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506157200

Carboxy-terminal region of Escherichia coli SecA ATPase is important to promote its protein translocation activity in vivo.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506157200

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.M506157200

PrlA4 prevents the rejection of signal sequence defective preproteins by stabilizing the SecA-SecY interaction during the initiation of translocation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506157200

Escherichia coli SecA truncated at its termini is functional and dimeric.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506157200

Reconstitution of Purified Bacterial Preprotein Translocase in Liposomes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M506157200

21 January 2018

Identifiers

DOI

10.1074/JBC.M506157200

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24 December 2017

PubMed ID

16115882

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24 December 2017