Following the leader: bacterial protein export through the Sec pathway. (Q33702236)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10431204%20AND%20SRC:MED&resulttype=core&format=json

10 December 2019

review article

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title

Following the leader: bacterial protein export through the Sec pathway (English)

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10431204%20AND%20SRC:MED&resulttype=core&format=json

10 December 2019

1

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10 December 2019

author name string

A Economou

series ordinal

1

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28 July 2017

publication date

1 August 1999

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10431204%20AND%20SRC:MED&resulttype=core&format=json

10 December 2019

published in

Trends in Microbiology

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10 December 2019

volume

7

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10 December 2019

issue

8

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10 December 2019

page(s)

315-320

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

10 December 2019

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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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SecB: a chaperone from Escherichia coli

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Calorimetric analyses of the interaction between SecB and its ligands

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Early events in preprotein recognition in E. coli: interaction of SRP and trigger factor with nascent polypeptides.

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The E. coli signal recognition particle is required for the insertion of a subset of inner membrane proteins

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The Escherichia coli SRP and SecB targeting pathways converge at the translocon

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

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Targeting of GroEL to SecA on the cytoplasmic membrane of Escherichia coli

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Involvement of the DnaK-DnaJ-GrpE chaperone team in protein secretion in Escherichia coli

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The bacterial SecY/E translocation complex forms channel-like structures similar to those of the eukaryotic Sec61p complex

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The JUN kinase/stress-activated protein kinase pathway is required for epidermal growth factor stimulation of growth of human A549 lung carcinoma cells.

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Escherichia coli SecA shape and dimensions

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

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SecY and SecA interact to allow SecA insertion and protein translocation across the Escherichia coli plasma membrane

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In vivo cross-linking of the SecA and SecY subunits of the Escherichia coli preprotein translocase

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7 January 2021

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

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Membrane deinsertion of SecA underlying proton motive force-dependent stimulation of protein translocation

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

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7 January 2021

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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7 January 2021

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

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7 January 2021

The role of anionic lipids in protein insertion and translocation in bacterial membranes

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7 January 2021

Erratum: Crystal structure of a bacterialsignal peptidase in complex with a β-lactam inhibitor

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Protein secretion and possible roles for multiple signal peptidases for precursor processing in bacilli

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SecDF of Bacillus subtilis, a molecular Siamese twin required for the efficient secretion of proteins.

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Signal peptides: exquisitely designed transport promoters

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Synthetic signal peptides specifically recognize SecA and stimulate ATPase activity in the absence of preprotein

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7 January 2021

Preprotein transfer to the Escherichia coli translocase requires the co‐operative binding of SecB and the signal sequence to SecA

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7 January 2021

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

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7 January 2021

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

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7 January 2021

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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7 January 2021

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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7 January 2021

Inhibition of preprotein translocation and reversion of the membrane inserted state of SecA by a carboxyl terminus binding mAb.

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7 January 2021

Interaction between SecA and SecYEG in Micellar Solution and Formation of the Membrane-Inserted State†

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7 January 2021

Roles of SecG in ATP- and SecA-dependent protein translocation.

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7 January 2021

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

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Translocase-Bound SecA Is Largely Shielded from the Phospholipid Acyl Chains†

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7 January 2021

Coupled structure changes of SecA and SecG revealed by the synthetic lethality of the secAcsR11 and delta secG::kan double mutant

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7 January 2021

Inversion of the membrane topology of SecG coupled with SecA-dependent preprotein translocation

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7 January 2021

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

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7 January 2021

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

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7 January 2021

The catalytic cycle of the escherichia coli SecA ATPase comprises two distinct preprotein translocation events

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7 January 2021

Protein folding in the bacterial periplasm

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Heterologous biopharmaceutical protein expression in Streptomyces

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Identifiers

DOI

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10 December 2019

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