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Trigger Factor can antagonize both SecB and DnaK/DnaJ chaperone functions in Escherichia coli

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/j.1460-2075.1991.tb07943.xopenalex-snapshot

Heat‐shock proteins can substitute for SecB function during protein export in Escherichia coli.

inferredcites →https://doi.org/10.1002/j.1460-2075.1994.tb06819.xopenalex-snapshot

Correlation between the structure and biochemical activities of FtsA, an essential cell division protein of the actin family.

inferredcites →https://doi.org/10.1007/pl00012488openalex-snapshot

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

inferredcites →https://doi.org/10.1007/s002030050732openalex-snapshot

Identification of Tn 10 insertions in the rfaG , rfaP , and galU genes involved in lipopolysaccharide core biosynthesis that affect Escherichia coli adhesion

inferredcites →https://doi.org/10.1016/0005-2736(87)90278-1openalex-snapshot

Optimal posttranslational translocation of the precursor of PhoE protein across Escherichia coli membrane vesicles requires both ATP and the protonmotive force

inferredcites →https://doi.org/10.1016/0022-2836(76)90119-4openalex-snapshot

Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu

inferredcites →https://doi.org/10.1016/0076-6879(91)04009-dopenalex-snapshot

[7] Uses of transposons with emphasis on Tn10

inferredcites →https://doi.org/10.1016/0092-8674(88)90116-xopenalex-snapshot

The “trigger factor cycle” includes ribosomes, presecretory proteins, and the plasma membrane

inferredcites →https://doi.org/10.1016/0092-8674(90)90160-gopenalex-snapshot

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

inferredcites →https://doi.org/10.1016/j.bbamcr.2004.02.009openalex-snapshot

The protein-conducting channel SecYEG

inferredcites →https://doi.org/10.1016/j.bbamcr.2004.03.013openalex-snapshot

SRP-mediated protein targeting: structure and function revisited

inferredcites →https://doi.org/10.1016/j.bbamcr.2004.06.003openalex-snapshot

Structure and function of SecA, the preprotein translocase nanomotor

inferredcites →https://doi.org/10.1016/j.cell.2005.05.028openalex-snapshot

Proteome-wide Analysis of Chaperonin-Dependent Protein Folding in Escherichia coli

inferredcites →https://doi.org/10.1016/j.febslet.2006.05.019openalex-snapshot

A model for co‐translational translocation: Ribosome‐regulated nascent polypeptide translocation at the protein‐conducting channel

inferredcites →https://doi.org/10.1016/s0014-5793(04)00052-3openalex-snapshot

Low temperature or GroEL/ES overproduction permits growth of Escherichia coli cells lacking trigger factor and DnaK

inferredcites →https://doi.org/10.1016/s0021-9258(19)84110-8openalex-snapshot

The C-terminal Domain of Escherichia coli Trigger Factor Represents the Central Module of Its Chaperone Activity

inferredcites →https://doi.org/10.1016/s0022-2836(02)01436-5openalex-snapshot

Localization of the Trigger Factor Binding Site on the Ribosomal 50S Subunit

inferredcites →https://doi.org/10.1016/s0092-8674(00)80787-4openalex-snapshot

Polypeptide Flux through Bacterial Hsp70

inferredcites →https://doi.org/10.1016/s0092-8674(00)80806-5openalex-snapshot

Getting Newly Synthesized Proteins into Shape

inferredcites →https://doi.org/10.1016/s0092-8674(00)80928-9openalex-snapshot

The Hsp70 and Hsp60 Chaperone Machines

inferredcites →https://doi.org/10.1016/s0092-8674(04)00299-5openalex-snapshot

Function of Trigger Factor and DnaK in Multidomain Protein Folding

inferredcites →https://doi.org/10.1038/23301openalex-snapshot

Trigger factor and DnaK cooperate in folding of newly synthesized proteins

inferredcites →https://doi.org/10.1038/nature01047openalex-snapshot

L23 protein functions as a chaperone docking site on the ribosome

inferredcites →https://doi.org/10.1038/nrm1492openalex-snapshot

Pathways of chaperone-mediated protein folding in the cytosol

inferredcites →https://doi.org/10.1038/sj.embor.7400067openalex-snapshot

In vivo analysis of the overlapping functions of DnaK and trigger factor

inferredcites →https://doi.org/10.1046/j.1365-2958.1997.6392003.xopenalex-snapshot

Expression of gpsA encoding biosynthetic sn‐glycerol 3‐phosphate dehydrogenase suppresses both the LB− phenotype of a secB null mutant and the cold‐sensitive phenotype of a secG null mutant

inferredcites →https://doi.org/10.1046/j.1365-2958.2001.02383.xopenalex-snapshot

Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol

inferredcites →https://doi.org/10.1073/pnas.0402398101openalex-snapshot

SecB is a bona fide generalized chaperone in Escherichia coli

inferredcites →https://doi.org/10.1073/pnas.100127597openalex-snapshot

An efficient recombination system for chromosome engineering in Escherichia coli

inferredcites →https://doi.org/10.1073/pnas.120163297openalex-snapshot

One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products

inferredcites →https://doi.org/10.1073/pnas.261432298openalex-snapshot

Binding specificity of Escherichia coli trigger factor

inferredcites →https://doi.org/10.1073/pnas.89.21.10341openalex-snapshot

Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli.

inferredcites →https://doi.org/10.1074/jbc.274.48.34219openalex-snapshot

Substrate Specificity of the SecB Chaperone

inferredcites →https://doi.org/10.1074/jbc.m205950200openalex-snapshot

Trigger Factor Retards Protein Export in Escherichia coli

inferredcites →https://doi.org/10.1074/jbc.m308025200openalex-snapshot

Two-stage Binding of SecA to the Bacterial Translocon Regulates Ribosome-Translocon Interaction

inferredcites →https://doi.org/10.1074/jbc.m313635200openalex-snapshot

Trigger Factor Peptidyl-prolyl cis/trans Isomerase Activity Is Not Essential for the Folding of Cytosolic Proteins in Escherichia coli

inferredcites →https://doi.org/10.1074/jbc.m509100200openalex-snapshot

Selective SecA Association with Signal Sequences in Ribosome-bound Nascent Chains

inferredcites →https://doi.org/10.1074/jbc.m509929200openalex-snapshot

Defining the Role of the Escherichia coli Chaperone SecB Using Comparative Proteomics

inferredcites →https://doi.org/10.1093/emboj/16.1.54openalex-snapshot

Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding

inferredcites →https://doi.org/10.1093/emboj/16.7.1501openalex-snapshot

Substrate specificity of the DnaK chaperone determined by screening cellulose‐bound peptide libraries

inferredcites →https://doi.org/10.1093/emboj/19.8.1900openalex-snapshot

Evolutionarily conserved binding of ribosomes to the translocation channel via the large ribosomal RNA

inferredcites →https://doi.org/10.1093/genetics/133.4.763openalex-snapshot

The Cs sec mutants of Escherichia coli reflect the cold sensitivity of protein export itself.

inferredcites →https://doi.org/10.1093/genetics/162.3.1045openalex-snapshot

Scanning Mutagenesis Identifies Amino Acid Residues Essential for the in Vivo Activity of the Escherichia coli DnaJ (Hsp40) J-Domain

inferredcites →https://doi.org/10.1101/gad.6.7.1165openalex-snapshot

DnaK and DnaJ heat shock proteins participate in protein export in Escherichia coli.

inferredcites →https://doi.org/10.1110/ps.062141006openalex-snapshot

Characterization of three areas of interactions stabilizing complexes between SecA and SecB, two proteins involved in protein export

inferredcites →https://doi.org/10.1126/science.277.5331.1453openalex-snapshot

The Complete Genome Sequence of Escherichia coli K-12

inferredcites →https://doi.org/10.1128/jb.154.1.253-260.1983openalex-snapshot

Mutations in a new gene, secB, cause defective protein localization in Escherichia coli

inferredcites →https://doi.org/10.1128/jb.163.1.267-274.1985openalex-snapshot

Evidence for specificity at an early step in protein export in Escherichia coli

inferredcites →https://doi.org/10.1128/jb.167.1.160-167.1986openalex-snapshot

Effects of signal sequence mutations on the kinetics of alkaline phosphatase export to the periplasm in Escherichia coli

inferredcites →https://doi.org/10.1128/jb.171.5.2337-2346.1989openalex-snapshot

Cellular defects caused by deletion of the Escherichia coli dnaK gene indicate roles for heat shock protein in normal metabolism

inferredcites →https://doi.org/10.1128/jb.178.12.3608-3613.1996openalex-snapshot

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

inferredcites →https://doi.org/10.1128/jb.178.21.6097-6104.1996openalex-snapshot

Influence of impaired chaperone or secretion function on SecB production in Escherichia coli

inferredcites →https://doi.org/10.1128/jb.183.19.5747-5750.2001openalex-snapshot

The djlA Gene Acts Synergistically with dnaJ in Promoting Escherichia coli Growth

inferredcites →https://doi.org/10.1128/jb.185.19.5697-5705.2003openalex-snapshot

Secretion of LamB-LacZ by the Signal Recognition Particle Pathway of Escherichia coli

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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inferred← citeshttps://doi.org/10.1002/jcb.25620openalex-snapshot

Global Analysis of the Impact of Deleting Trigger Factor on the Transcriptome Profile of Escherichia coli

inferred← citeshttps://doi.org/10.1002/mbo3.9openalex-snapshot

The C‐tail anchored TssL subunit, an essential protein of the enteroaggregative Escherichia coli Sci‐1 Type VI secretion system, is inserted by YidC

inferred← citeshttps://doi.org/10.1002/pro.3161openalex-snapshot

The chaperone toolbox at the single‐molecule level: From clamping to confining

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Recycling and Tinkering: The Evolution of Protein Transport to and into Endosymbiotically Derived Organelles

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Mechanistic insight into co-translational protein processing, folding, targeting, and membrane insertion

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Toward Complexity

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TAC from Mycobacterium tuberculosis: a paradigm for stress-responsive toxin–antitoxin systems controlled by SecB-like chaperones

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The evolution of protein targeting and translocation systems

inferred← citeshttps://doi.org/10.1016/j.bbamcr.2013.11.007openalex-snapshot

Chaperone networking facilitates protein targeting to the bacterial cytoplasmic membrane

inferred← citeshttps://doi.org/10.1016/j.bbamcr.2014.02.014openalex-snapshot

SecA-mediated targeting and translocation of secretory proteins

inferred← citeshttps://doi.org/10.1016/j.cell.2011.10.044openalex-snapshot

Selective Ribosome Profiling Reveals the Cotranslational Chaperone Action of Trigger Factor In Vivo

inferred← citeshttps://doi.org/10.1016/j.celrep.2011.12.007openalex-snapshot

DnaK Functions as a Central Hub in the E. coli Chaperone Network

inferred← citeshttps://doi.org/10.1016/j.celrep.2022.111776openalex-snapshot

Selective ribosome profiling reveals a role for SecB in the co-translational inner membrane protein biogenesis

inferred← citeshttps://doi.org/10.1016/j.enzmictec.2025.110778openalex-snapshot

Revolutionizing recombinant protein production in prokaryotic platforms – Methodologies and advances

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System analysis of salt and osmotic stress induced proteins in Nostoc muscorum and Bradyrhizobium japonicum

inferred← citeshttps://doi.org/10.1016/j.jmb.2008.10.094openalex-snapshot

SecB-Mediated Protein Export Need Not Occur via Kinetic Partitioning

inferred← citeshttps://doi.org/10.1016/j.jmb.2017.12.004openalex-snapshot

SRP, FtsY, DnaK and YidC Are Required for the Biogenesis of the E. coli Tail-Anchored Membrane Proteins DjlC and Flk

inferred← citeshttps://doi.org/10.1016/j.micres.2016.03.001openalex-snapshot

Large-scale gene expression profiling reveals physiological response to deletion of chaperone dnaKJ in Escherichia coli

inferred← citeshttps://doi.org/10.1016/j.molcel.2010.12.028openalex-snapshot

SecA Interacts with Ribosomes in Order to Facilitate Posttranslational Translocation in Bacteria

inferred← citeshttps://doi.org/10.1016/j.molcel.2021.05.016openalex-snapshot

Bacterial RF3 Senses Chaperone Function in Co-Translational Folding

inferred← citeshttps://doi.org/10.1016/j.pep.2010.06.008openalex-snapshot

Enhancing the secretory yields of leech carboxypeptidase inhibitor in Escherichia coli: Influence of trigger factor and signal recognition particle

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The effects of overexpression of cytoplasmic chaperones on secretory production of hirudin-PA in E. coli

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Long-Lived Folding Intermediates Predominate the Targeting-Competent Secretome

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Tripartite toxin–antitoxin systems: expanding the paradigm of molecular interplay and antiphage defense

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Unique Structural Modulation of a Non-Native Substrate by Cochaperone DnaJ

inferred← citeshttps://doi.org/10.1021/bi800233wopenalex-snapshot

The Periplasmic Chaperone PpiD Interacts with Secretory Proteins Exiting from the SecYEG Translocon

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Structural basis for the antifolding activity of a molecular chaperone

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Chaperone addiction of toxin–antitoxin systems

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Delivering proteins for export from the cytosol

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Protein export through the bacterial Sec pathway

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The ribosome as a platform for co-translational processing, folding and targeting of newly synthesized proteins

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Structural insights into chaperone addiction of toxin-antitoxin systems

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Ribosome profiling reveals multiple roles of SecA in cotranslational protein export

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Cold adaptation in the environmental bacterium Shewanella oneidensis is controlled by a J-domain co-chaperone protein network

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Understanding the relationships between solubility, stability, and activity of silicatein

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SecB-like chaperone controls a toxin–antitoxin stress-responsive system in Mycobacterium tuberculosis

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Directed evolution of SecB chaperones toward toxin-antitoxin systems

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Adaptability of the GroEL/GroES chaperonin to proteostatic challenge revealed by directed evolution

inferred← citeshttps://doi.org/10.1074/jbc.m110.133058openalex-snapshot

Lon Protease Quality Control of Presecretory Proteins in Escherichia coli and Its Dependence on the SecB and DnaJ (Hsp40) Chaperones

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The Rate of Folding Dictates Substrate Secretion by the Escherichia coli Hemolysin Type 1 Secretion System

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Conserved, Disordered C Terminus of DnaK Enhances Cellular Survival upon Stress and DnaK in Vitro Chaperone Activity

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Hsp33 Controls Elongation Factor-Tu Stability and Allows Escherichia coli Growth in the Absence of the Major DnaK and Trigger Factor Chaperones

inferred← citeshttps://doi.org/10.1093/femsle/fny093openalex-snapshot

The way is the goal: how SecA transports proteins across the cytoplasmic membrane in bacteria

inferred← citeshttps://doi.org/10.1096/fj.201701576openalex-snapshot

Exploring the roles of substrate‐binding surface of the chaperone site in the chaperone activity of trigger factor

inferred← citeshttps://doi.org/10.1099/mic.0.050880-0openalex-snapshot

Redundancy and specificity of multiple trigger factor chaperones in Desulfitobacteria

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AscA (YecA) is a molecular chaperone involved in Sec-dependent protein translocation in Escherichia coli

inferred← citeshttps://doi.org/10.1111/j.1365-2958.2007.05961.xopenalex-snapshot

The Hsp70 chaperone machines of Escherichia coli: a paradigm for the repartition of chaperone functions

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Physical map and dynamics of the chaperone network in Escherichia coli

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Cold adaptation in the marine bacterium, Sphingopyxis alaskensis , assessed using quantitative proteomics

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Proteome analysis at the subcellular level of the cyanobacteriumSpirulina platensisin response to low-temperature stress conditions

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Structural Basis for Protein Antiaggregation Activity of the Trigger Factor Chaperone

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SecA Cotranslationally Interacts with Nascent Substrate Proteins In Vivo

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Trigger Factor from the Psychrophilic Bacterium Psychrobacter frigidicola Is a Monomeric Chaperone

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Subcellular proteomic characterization of the high-temperature stress response of the cyanobacterium Spirulina platensis

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Large-Scale Evolutionary Analyses on SecB Subunits of Bacterial Sec System

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Trigger factor is a bona fide secretory pathway chaperone that interacts with SecB and the translocase

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Multitasking SecB chaperones in bacteria

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Oligomerization of a molecular chaperone modulates its activity

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