Bacterial preprotein translocase: mechanism and conformational dynamics of a processive enzyme. (Q41715787)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9489663%20AND%20SRC:MED&resulttype=core&format=json

9 November 2019

review article

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title

Bacterial preprotein translocase: mechanism and conformational dynamics of a processive enzyme (English)

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9 November 2019

1

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9 November 2019

author name string

A Economou

series ordinal

1

1 reference

7 October 2017

language of work or name

English

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publication date

1 February 1998

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9489663%20AND%20SRC:MED&resulttype=core&format=json

9 November 2019

published in

Molecular Microbiology

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9 November 2019

volume

27

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9 November 2019

issue

3

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9 November 2019

page(s)

511-518

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Protein translocation in Escherichia coli.

9 November 2019

cites work

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

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A significant fraction of functional SecA is permanently embedded in the membrane. SecA cycling on and off the membrane is not essential during protein translocation.

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Secretory proteins move through the endoplasmic reticulum membrane via an aqueous, gated pore.

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Domain interactions of the peripheral preprotein Translocase subunit SecA.

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Bacterial protein translocation: kinetic and thermodynamic role of ATP and the protonmotive force

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

21 January 2018

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

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

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

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

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The protease-protected 30 kDa domain of SecA is largely inaccessible to the membrane lipid phase

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

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Subunit dynamics in Escherichia coli preprotein translocase

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

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

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prlA suppressors in Escherichia coli relieve the proton electrochemical gradient dependency of translocation of wild-type precursors

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SecA protein: autoregulated ATPase catalysing preprotein insertion and translocation across the Escherichia coli inner membrane

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RNA helicase activity of Escherichia coli SecA protein.

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Genetic and molecular characterization of the Escherichia coli secD operon and its products

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In vivo analyses of interactions between SecE and SecY, core components of the Escherichia coli protein translocation machinery.

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

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High selectivity with low specificity: how SecB has solved the paradox of chaperone binding

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SecF stabilizes SecD and SecY, components of the protein translocation machinery of the Escherichia coli cytoplasmic membrane

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

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Identification of a region of interaction between Escherichia coli SecA and SecY proteins.

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Stepwise movement of preproteins in the process of translocation across the cytoplasmic membrane of Escherichia coli.

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

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SecA protein is required for translocation of a model precursor protein into inverted vesicles of Escherichia coli plasma membrane

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Escherichia coli preprotein translocase

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SecE-depleted membranes of Escherichia coli are active. SecE is not obligatorily required for the in vitro translocation of certain protein precursors.

21 January 2018

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Oligomeric Rings of the Sec61p Complex Induced by Ligands Required for Protein Translocation

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Separable ATPase and Membrane Insertion Domains of the SecA Subunit of Preprotein Translocase

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