Bacterial protein secretion through the translocase nanomachine (Q36972407)

17 August 2017

1 reference

title

Bacterial protein secretion through the translocase nanomachine (English)

1 reference

17 August 2017

Effrosyni Papanikou

1

1 reference

17 August 2017

Spyridoula Karamanou

series ordinal

2

1 reference

17 August 2017

Anastassios Economou

series ordinal

3

1 reference

17 August 2017

language of work or name

English

0 references

publication date

1 November 2007

1 reference

Nature Reviews Microbiology

17 August 2017

1 reference

17 August 2017

5

1 reference

17 August 2017

11

1 reference

17 August 2017

839-851

1 reference

https://scigraph.springernature.com/pub.10.1038/nrmicro1771

17 August 2017

0 references

cites work

NMR structure of the C-terminal domain of SecA in the free state.

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Amino-terminal region of SecA is involved in the function of SecG for protein translocation into Escherichia coli membrane vesicles.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Membrane topology inversion of SecG detected by labeling with a membrane-impermeable sulfhydryl reagent that causes a close association of SecG with SecA.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Sec-dependent membrane protein insertion: sequential interaction of nascent FtsQ with SecY and YidC.

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Secretion by numbers: Protein traffic in prokaryotes

21 January 2018

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Translocation of bacterial proteins--an overview

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

X-ray structure of a protein-conducting channel

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

The plug domain of the SecY protein stabilizes the closed state of the translocation channel and maintains a membrane seal

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Architecture of the protein-conducting channel associated with the translating 80S ribosome.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Alignment of conduits for the nascent polypeptide chain in the ribosome-Sec61 complex

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

A large conformational change of the translocation ATPase SecA

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

A novel dimer interface and conformational changes revealed by an X-ray structure of B. subtilis SecA

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Structure of dimeric SecA, the Escherichia coli preprotein translocase motor

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Crystal structure of Mycobacterium tuberculosis SecA, a preprotein translocating ATPase

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Crystal structure of the translocation ATPase SecA from Thermus thermophilus reveals a parallel, head-to-head dimer.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

SecB is a bona fide generalized chaperone in Escherichia coli

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

The DsbA signal sequence directs efficient, cotranslational export of passenger proteins to the Escherichia coli periplasm via the signal recognition particle pathway

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Signal Recognition Particle (SRP)-mediated Targeting and Sec-dependent Translocation of an ExtracellularEscherichia coliProtein

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Translocation of domains of nascent periplasmic proteins across the cytoplasmic membrane is independent of elongation

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

SecA Is Not Required for Signal Recognition Particle-mediated Targeting and Initial Membrane Insertion of a Nascent Inner Membrane Protein

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

SRP-dependent co-translational targeting and SecA-dependent translocation analyzed as individual steps in the export of a bacterial protein

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Interactions between folding factors and bacterial outer membrane proteins

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Catalysis of disulfide bond formation and isomerization in the Escherichia coli periplasm

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Protein disulfide isomerase: the structure of oxidative folding

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Atomic Model of the E.coli Membrane-bound Protein Translocation Complex SecYEG

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

One of three transmembrane stretches is sufficient for the functioning of the SecE protein, a membrane component of the E. coli secretion machinery.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Determining the conductance of the SecY protein translocation channel for small molecules

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

The sec and prl genes of Escherichia coli

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

A signal sequence is not required for protein export in prlA mutants of Escherichia coli

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Signal sequence recognition in posttranslational protein transport across the yeast ER membrane.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Investigating the SecY plug movement at the SecYEG translocation channel.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Deregulation of the SecYEG translocation channel upon removal of the plug domain.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

The plug domain of yeast Sec61p is important for efficient protein translocation, but is not essential for cell viability

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Molecular dynamics studies of the archaeal translocon

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Nanodiscs unravel the interaction between the SecYEG channel and its cytosolic partner SecA.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Fluorescence resonance energy transfer analysis of protein translocase. SecYE from Thermus thermophilus HB8 forms a constitutive oligomer in membranes.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

The aqueous pore through the translocon has a diameter of 40-60 A during cotranslational protein translocation at the ER membrane

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Protein translocation is mediated by oligomers of the SecY complex with one SecY copy forming the channel.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Identification of the preprotein binding domain of SecA.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Disorder-order folding transitions underlie catalysis in the helicase motor of SecA

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

The DEAD-box protein family of RNA helicases

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

The long alpha-helix of SecA is important for the ATPase coupling of translocation.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Solution NMR structure and X-ray absorption analysis of the C-terminal zinc-binding domain of the SecA ATPase

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Zinc stabilizes the SecB binding site of SecA.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Selective photoaffinity labeling identifies the signal peptide binding domain on SecA

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Preprotein-controlled catalysis in the helicase motor of SecA

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Complex behavior in solution of homodimeric SecA.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Escherichia coli SecA shape and dimensions

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Quantitative renaturation from a guanidine-denatured state of the SecA dimer, a 200 KDa protein involved in protein secretion in Escherichia coli

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

The ATPase domain of SecA can form a tetramer in solution.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

The carboxyl-terminal region is essential for Sec-A dimerization

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Different modes of SecY-SecA interactions revealed by site-directed in vivo photo-cross-linking

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Identification of Two Interaction Sites in SecY that Are Important for the Functional Interaction with SecA

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Preferential interaction of Sec-G with Sec-E stabilizes an unstable Sec-E derivative in the Escherichia coli cytoplasmic membrane.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Distinct membrane binding properties of N- and C-terminal domains of Escherichia coli SecA ATPase

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Covalently dimerized SecA is functional in protein translocation

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Projection structure and oligomeric properties of a bacterial core protein translocase

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

SecD and SecF facilitate protein export in Escherichia coli.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Oxa1/Alb3/YidC system for insertion of membrane proteins in mitochondria, chloroplasts and bacteria (review).

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Escherichia coli YidC is a membrane insertase for Sec-independent proteins

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

YidC, an assembly site for polytopic Escherichia coli membrane proteins located in immediate proximity to the SecYE translocon and lipids

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

SecDFyajC forms a heterotetrameric complex with YidC.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

The role of lipids in membrane insertion and translocation of bacterial proteins

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Increases in acidic phospholipid contents specifically restore protein translocation in a cold-sensitive secA or secG null mutant

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Crystal structure of the bacterial protein export chaperone secB

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Structural determinants of SecB recognition by SecA in bacterial protein translocation

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Crystal structure of SecB from Escherichia coli

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

The interaction between the chaperone SecB and its ligands: evidence for multiple subsites for binding

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Substrate specificity of the SecB chaperone

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Complexes between protein export chaperone SecB and SecA. Evidence for separate sites on SecA providing binding energy and regulatory interactions

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Mapping of the docking of SecA onto the chaperone SecB by site-directed spin labeling: insight into the mechanism of ligand transfer during protein export

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Ligand crowding at a nascent signal sequence

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

The conformation of a signal peptide bound by Escherichia coli preprotein translocase SecA

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Tyr-326 plays a critical role in controlling SecA-preprotein interaction

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Purification of a functional mature region from a SecA-dependent preprotein

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Nucleotide exchange from the high-affinity ATP-binding site in SecA is the rate-limiting step in the ATPase cycle of the soluble enzyme and occurs through a specialized conformational state

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

The SecYEG preprotein translocation channel is a conformationally dynamic and dimeric structure

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

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

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Translocation can drive the unfolding of a preprotein domain.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

The spontaneous insertion of proteins into and across membranes: the helical hairpin hypothesis

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

The SecA and SecY subunits of translocase are the nearest neighbors of a translocating preprotein, shielding it from phospholipids

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Transmembrane helices before, during, and after insertion

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Hydrophobic forces drive spontaneous membrane insertion of the bacteriophage Pf3 coat protein without topological control

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

F1F0 ATP synthase subunit c is a substrate of the novel YidC pathway for membrane protein biogenesis

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Structure of the membrane protein FhaC: a member of the Omp85-TpsB transporter superfamily.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Structure and function of an essential component of the outer membrane protein assembly machine

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Biogenesis of the gram-negative bacterial outer membrane.

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

Sites of interaction of a precursor polypeptide on the export chaperone SecB mapped by site-directed spin labeling

31 March 2020

1 reference

https://api.crossref.org/works/10.1038%2FNRMICRO1771

31 March 2020

Identifiers

DOI

10.1038/NRMICRO1771

1 reference

17 August 2017

1 reference