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

PubWeight™: 1.42‹?› | Rank: Top 5%

🔗 View Article (PMC 1298978)

Published in EMBO Rep on January 09, 2004

Authors

Pierre Genevaux1, France Keppel, Françoise Schwager, Petra S Langendijk-Genevaux, F Ulrich Hartl, Costa Georgopoulos

Author Affiliations

1: Département de Biochimie Médicale, Centre Médical Universitaire, Genève, Switzerland. pierre.genevaux@medecine.unige.ch

Articles citing this

Structural basis for protein antiaggregation activity of the trigger factor chaperone. Science (2014) 1.86

Chain dynamics of nascent polypeptides emerging from the ribosome. ACS Chem Biol (2008) 1.59

Strain engineering for improved expression of recombinant proteins in bacteria. Microb Cell Fact (2011) 1.36

Promiscuous substrate recognition in folding and assembly activities of the trigger factor chaperone. Cell (2009) 1.32

Construction of a large signature-tagged mini-Tn5 transposon library and its application to mutagenesis of Sinorhizobium meliloti. Appl Environ Microbiol (2006) 1.31

Structure of trigger factor binding domain in biologically homologous complex with eubacterial ribosome reveals its chaperone action. Proc Natl Acad Sci U S A (2005) 1.24

Cotranslational folding promotes beta-helix formation and avoids aggregation in vivo. J Mol Biol (2008) 1.21

SecB is a bona fide generalized chaperone in Escherichia coli. Proc Natl Acad Sci U S A (2004) 1.16

Physiologic effects of forced down-regulation of dnaK and groEL expression in Streptococcus mutans. J Bacteriol (2006) 1.16

Trigger Factor can antagonize both SecB and DnaK/DnaJ chaperone functions in Escherichia coli. Proc Natl Acad Sci U S A (2007) 1.11

Toothpicks, serendipity and the emergence of the Escherichia coli DnaK (Hsp70) and GroEL (Hsp60) chaperone machines. Genetics (2006) 1.09

GroES/GroEL and DnaK/DnaJ have distinct roles in stress responses and during cell cycle progression in Caulobacter crescentus. J Bacteriol (2006) 1.09

Global analysis of chaperone effects using a reconstituted cell-free translation system. Proc Natl Acad Sci U S A (2012) 1.05

Towards the development of Bacillus subtilis as a cell factory for membrane proteins and protein complexes. Microb Cell Fact (2008) 1.05

SecB-like chaperone controls a toxin-antitoxin stress-responsive system in Mycobacterium tuberculosis. Proc Natl Acad Sci U S A (2011) 1.00

Secretion of GOB metallo-beta-lactamase in Escherichia coli depends strictly on the cooperation between the cytoplasmic DnaK chaperone system and the Sec machinery: completion of folding and Zn(II) ion acquisition occur in the bacterial periplasm. Antimicrob Agents Chemother (2009) 0.96

Versatility of trigger factor interactions with ribosome-nascent chain complexes. J Biol Chem (2010) 0.91

Why molecular chaperones buffer mutational damage: a case study with a yeast Hsp40/70 system. Genetics (2006) 0.90

Protein folding on the ribosome studied using NMR spectroscopy. Prog Nucl Magn Reson Spectrosc (2013) 0.87

Hsp33 controls elongation factor-Tu stability and allows Escherichia coli growth in the absence of the major DnaK and trigger factor chaperones. J Biol Chem (2012) 0.86

Lon protease quality control of presecretory proteins in Escherichia coli and its dependence on the SecB and DnaJ (Hsp40) chaperones. J Biol Chem (2010) 0.86

The Hsp40 J-domain stimulates Hsp70 when tethered by the client to the ATPase domain. J Biol Chem (2010) 0.84

Identification of a potential hydrophobic peptide binding site in the C-terminal arm of trigger factor. Protein Sci (2007) 0.84

Integrating protein homeostasis strategies in prokaryotes. Cold Spring Harb Perspect Biol (2011) 0.83

DnaJ (Hsp40 protein) binding to folded substrate impacts KplE1 prophage excision efficiency. J Biol Chem (2012) 0.82

Trigger factor finds new jobs and contacts. Nat Struct Mol Biol (2009) 0.81

Fine-mapping the contact sites of the Escherichia coli cell division proteins FtsB and FtsL on the FtsQ protein. J Biol Chem (2013) 0.80

Multitasking SecB chaperones in bacteria. Front Microbiol (2014) 0.79

Flexibility of the bacterial chaperone trigger factor in microsecond-timescale molecular dynamics simulations. Biophys J (2013) 0.78

Trigger factor from the psychrophilic bacterium Psychrobacter frigidicola is a monomeric chaperone. J Bacteriol (2008) 0.77

Functional conservation and divergence of J-domain-containing ZUO1/ZRF orthologs throughout evolution. Planta (2014) 0.77

Construction and complementation of in-frame deletions of the essential Escherichia coli thymidylate kinase gene. Appl Environ Microbiol (2006) 0.77

Keeping up with protein folding. Microb Cell Fact (2004) 0.77

Stress down south: meeting report of the fifth International Workshop on the Molecular Biology of Stress Responses. Cell Stress Chaperones (2006) 0.76

Reconstitution of a Mycobacterium tuberculosis proteostasis network highlights essential cofactor interactions with chaperone DnaK. Proc Natl Acad Sci U S A (2016) 0.76

Chaperone addiction of toxin-antitoxin systems. Nat Commun (2016) 0.75

Study on the chaperone properties of conserved GTPases. Protein Cell (2012) 0.75

Multilevel interaction of the DnaK/DnaJ(HSP70/HSP40) stress-responsive chaperone machine with the central metabolism. Sci Rep (2017) 0.75

Articles cited by this

The complete genome sequence of Escherichia coli K-12. Science (1997) 84.27

Pedigrees of some mutant strains of Escherichia coli K-12. Bacteriol Rev (1972) 35.97

Transposition and fusion of the lac genes to selected promoters in Escherichia coli using bacteriophage lambda and Mu. J Mol Biol (1976) 33.01

Molecular chaperones in the cytosol: from nascent chain to folded protein. Science (2002) 15.09

Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding. Nature (1992) 5.92

Trigger factor: a soluble protein that folds pro-OmpA into a membrane-assembly-competent form. Proc Natl Acad Sci U S A (1987) 2.97

Trigger factor and DnaK cooperate in folding of newly synthesized proteins. Nature (1999) 2.95

Identification of in vivo substrates of the chaperonin GroEL. Nature (1999) 2.95

L23 protein functions as a chaperone docking site on the ribosome. Nature (2002) 2.68

Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol. Mol Microbiol (2001) 2.54

Early events in preprotein recognition in E. coli: interaction of SRP and trigger factor with nascent polypeptides. EMBO J (1995) 2.38

Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains. Cell (1999) 2.33

Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli. Proc Natl Acad Sci U S A (1992) 2.04

In vivo observation of polypeptide flux through the bacterial chaperonin system. Cell (1997) 1.99

Trigger Factor and DnaK possess overlapping substrate pools and binding specificities. Mol Microbiol (2003) 1.77

Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains. Proc Natl Acad Sci U S A (1996) 1.69

A functional chaperone triad on the yeast ribosome. Proc Natl Acad Sci U S A (2002) 1.63

Trigger factor depletion or overproduction causes defective cell division but does not block protein export. J Bacteriol (1990) 1.59

Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding. EMBO J (1997) 1.49

Binding specificity of Escherichia coli trigger factor. Proc Natl Acad Sci U S A (2001) 1.45

Trigger factor is involved in GroEL-dependent protein degradation in Escherichia coli and promotes binding of GroEL to unfolded proteins. EMBO J (1995) 1.34

Prevention and reversion of protein aggregation by molecular chaperones in the E. coli cytosol: implications for their applicability in biotechnology. J Biotechnol (2002) 1.34

Trigger factor retards protein export in Escherichia coli. J Biol Chem (2002) 1.33

The Fe/S assembly protein IscU behaves as a substrate for the molecular chaperone Hsc66 from Escherichia coli. J Biol Chem (2000) 1.30

Trigger factor-mediated prolyl isomerization influences maturation of the Streptococcus pyogenes cysteine protease. J Bacteriol (2003) 1.24

Protein traffic in bacteria: multiple routes from the ribosome to and across the membrane. Prog Nucleic Acid Res Mol Biol (2001) 1.22

The amino-terminal 118 amino acids of Escherichia coli trigger factor constitute a domain that is necessary and sufficient for binding to ribosomes. J Biol Chem (1997) 1.20

Dynamic association of trigger factor with protein substrates. J Mol Biol (2001) 1.11

The djlA gene acts synergistically with dnaJ in promoting Escherichia coli growth. J Bacteriol (2001) 0.97

Structure-function analysis of HscC, the Escherichia coli member of a novel subfamily of specialized Hsp70 chaperones. J Biol Chem (2002) 0.85

Articles by these authors

New developments in the InterPro database. Nucleic Acids Res (2007) 12.49

Recent improvements to the PROSITE database. Nucleic Acids Res (2004) 11.89

The PROSITE database. Nucleic Acids Res (2006) 8.11

PROSITE, a protein domain database for functional characterization and annotation. Nucleic Acids Res (2009) 7.47

Pathways of chaperone-mediated protein folding in the cytosol. Nat Rev Mol Cell Biol (2004) 6.45

ScanProsite: detection of PROSITE signature matches and ProRule-associated functional and structural residues in proteins. Nucleic Acids Res (2006) 6.13

The 20 years of PROSITE. Nucleic Acids Res (2007) 6.06

Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli. Cell (2005) 4.78

A stress sensor for the bacterial periplasm. Cell (2003) 4.52

Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70. Cell (2003) 4.46

Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions. Cell (2011) 3.98

Protein abundance profiling of the Escherichia coli cytosol. BMC Genomics (2008) 3.78

Molecular chaperone functions in protein folding and proteostasis. Annu Rev Biochem (2013) 3.56

Structural features of the GroEL-GroES nano-cage required for rapid folding of encapsulated protein. Cell (2006) 3.45

ProRule: a new database containing functional and structural information on PROSITE profiles. Bioinformatics (2005) 3.41

Protein quality control during aging involves recruitment of the macroautophagy pathway by BAG3. EMBO J (2009) 2.83

Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding. Cell (2008) 2.80

Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s. EMBO J (2006) 2.58

Protein synthesis upon acute nutrient restriction relies on proteasome function. Science (2005) 2.32

Chaperones increase association of tau protein with microtubules. Proc Natl Acad Sci U S A (2003) 2.32

Real-time observation of trigger factor function on translating ribosomes. Nature (2006) 2.23

A balance of protein synthesis and proteasome-dependent degradation determines the maintenance of LTP. Neuron (2006) 2.23

Role of the myosin assembly protein UNC-45 as a molecular chaperone for myosin. Science (2002) 2.22

Cellular toxicity of polyglutamine expansion proteins: mechanism of transcription factor deactivation. Mol Cell (2004) 2.19

Hereditary spastic paraplegia SPG13 is associated with a mutation in the gene encoding the mitochondrial chaperonin Hsp60. Am J Hum Genet (2002) 2.17

Chaperonin TRiC promotes the assembly of polyQ expansion proteins into nontoxic oligomers. Mol Cell (2006) 2.16

Roles of molecular chaperones in protein misfolding diseases. Semin Cell Dev Biol (2004) 2.14

Structure and function of RbcX, an assembly chaperone for hexadecameric Rubisco. Cell (2007) 2.11

Ligand discrimination by TPR domains. Relevance and selectivity of EEVD-recognition in Hsp70 x Hop x Hsp90 complexes. J Biol Chem (2002) 2.04

Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange. Mol Cell (2005) 1.94

The native 3D organization of bacterial polysomes. Cell (2009) 1.88

The Hsp70 chaperone machines of Escherichia coli: a paradigm for the repartition of chaperone functions. Mol Microbiol (2007) 1.87

Function of trigger factor and DnaK in multidomain protein folding: increase in yield at the expense of folding speed. Cell (2004) 1.85

The cellular prion protein mediates neurotoxic signalling of β-sheet-rich conformers independent of prion replication. EMBO J (2011) 1.80

The molecular architecture of the eukaryotic chaperonin TRiC/CCT. Structure (2012) 1.80

PolyQ proteins interfere with nuclear degradation of cytosolic proteins by sequestering the Sis1p chaperone. Cell (2013) 1.76

Protein folding in the cytoplasm and the heat shock response. Cold Spring Harb Perspect Biol (2010) 1.71

The role of molecular chaperones in human misfolding diseases. FEBS Lett (2009) 1.68

Molecular chaperones as modulators of polyglutamine protein aggregation and toxicity. Proc Natl Acad Sci U S A (2002) 1.65

Coupled chaperone action in folding and assembly of hexadecameric Rubisco. Nature (2010) 1.63

Isolation and characterization of biofilm formation-defective mutants of Staphylococcus aureus. Infect Immun (2006) 1.58

DnaK functions as a central hub in the E. coli chaperone network. Cell Rep (2012) 1.52

Retracted L25 functions as a conserved ribosomal docking site shared by nascent chain-associated complex and signal-recognition particle. EMBO Rep (2006) 1.51

Mitochondrial hsp60 chaperonopathy causes an autosomal-recessive neurodegenerative disorder linked to brain hypomyelination and leukodystrophy. Am J Hum Genet (2008) 1.49

Monitoring protein conformation along the pathway of chaperonin-assisted folding. Cell (2008) 1.45

Retracted TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes. EMBO J (2003) 1.38

Chaperonin-catalyzed rescue of kinetically trapped states in protein folding. Cell (2010) 1.36

Firefly luciferase mutants as sensors of proteome stress. Nat Methods (2011) 1.35

Scanning mutagenesis identifies amino acid residues essential for the in vivo activity of the Escherichia coli DnaJ (Hsp40) J-domain. Genetics (2002) 1.30

Essential role of the chaperonin folding compartment in vivo. EMBO J (2008) 1.29

The three-dimensional organization of polyribosomes in intact human cells. Mol Cell (2010) 1.26

Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system. EMBO J (2003) 1.25

Structure and function of the AAA+ protein CbbX, a red-type Rubisco activase. Nature (2011) 1.20

Essential role of the unusual DNA-binding motif of BAG-1 for inhibition of the glucocorticoid receptor. J Biol Chem (2002) 1.19

Structure of hibernating ribosomes studied by cryoelectron tomography in vitro and in situ. J Cell Biol (2010) 1.19

Proteolytic cleavage of polyglutamine-expanded ataxin-3 is critical for aggregation and sequestration of non-expanded ataxin-3. Hum Mol Genet (2006) 1.18

SecB is a bona fide generalized chaperone in Escherichia coli. Proc Natl Acad Sci U S A (2004) 1.16

Mitochondrial stress signaling: a pathway unfolds. Trends Cell Biol (2007) 1.16

De novo folding of GFP fusion proteins: high efficiency in eukaryotes but not in bacteria. J Mol Biol (2005) 1.15

Advancing cell biology through proteomics in space and time (PROSPECTS). Mol Cell Proteomics (2012) 1.15

The role of the DIF motif of the DnaJ (Hsp40) co-chaperone in the regulation of the DnaK (Hsp70) chaperone cycle. J Biol Chem (2006) 1.12

Quantitative proteomics reveals that Hsp90 inhibition preferentially targets kinases and the DNA damage response. Mol Cell Proteomics (2011) 1.12

Trigger Factor can antagonize both SecB and DnaK/DnaJ chaperone functions in Escherichia coli. Proc Natl Acad Sci U S A (2007) 1.11

Identification of nascent chain interaction sites on trigger factor. J Biol Chem (2007) 1.11

Calpain inhibition is sufficient to suppress aggregation of polyglutamine-expanded ataxin-3. J Biol Chem (2007) 1.07

SnapShot: molecular chaperones, Part I. Cell (2007) 1.05

Structure of green-type Rubisco activase from tobacco. Nat Struct Mol Biol (2011) 1.05

Identification of anti-prion compounds as efficient inhibitors of polyglutamine protein aggregation in a zebrafish model. J Biol Chem (2006) 1.03

Exploring the capacity of trigger factor to function as a shield for ribosome bound polypeptide chains. FEBS Lett (2005) 1.03

A novel mutation in the HSPD1 gene in a patient with hereditary spastic paraplegia. J Neurol (2007) 1.02

The Hsp60-(p.V98I) mutation associated with hereditary spastic paraplegia SPG13 compromises chaperonin function both in vitro and in vivo. J Biol Chem (2008) 1.02

Crystal structure of an archaeal actin homolog. J Mol Biol (2006) 1.00

The heat shock protein 90-targeting drug cisplatin selectively inhibits steroid receptor activation. Mol Endocrinol (2003) 1.00

Physicochemical determinants of chaperone requirements. J Mol Biol (2010) 0.99

Systematic identification of antiprion drugs by high-throughput screening based on scanning for intensely fluorescent targets. J Virol (2005) 0.97

Inhibition of GR-mediated transcription by p23 requires interaction with Hsp90. FEBS Lett (2004) 0.97

Folding of large multidomain proteins by partial encapsulation in the chaperonin TRiC/CCT. Proc Natl Acad Sci U S A (2012) 0.95

The UBXN-2/p37/p47 adaptors of CDC-48/p97 regulate mitosis by limiting the centrosomal recruitment of Aurora A. J Cell Biol (2013) 0.95

Crystal structure of a chaperone-bound assembly intermediate of form I Rubisco. Nat Struct Mol Biol (2011) 0.95

Interaction of the Hsp110 molecular chaperones from S. cerevisiae with substrate protein. J Mol Biol (2010) 0.94

SnapShot: molecular chaperones, Part II. Cell (2007) 0.93

Differential substrate specificity of group I and group II chaperonins in the archaeon Methanosarcina mazei. Mol Microbiol (2009) 0.93

Fes1p acts as a nucleotide exchange factor for the ribosome-associated molecular chaperone Ssb1p. Biol Chem (2006) 0.93

Coexistence of group I and group II chaperonins in the archaeon Methanosarcina mazei. J Biol Chem (2003) 0.93

Versatility of trigger factor interactions with ribosome-nascent chain complexes. J Biol Chem (2010) 0.91

The Escherichia coli DjlA and CbpA proteins can substitute for DnaJ in DnaK-mediated protein disaggregation. J Bacteriol (2004) 0.90

Bacteriophage-encoded cochaperonins can substitute for Escherichia coli's essential GroES protein. EMBO Rep (2002) 0.87

Chaperonin cofactors, Cpn10 and Cpn20, of green algae and plants function as hetero-oligomeric ring complexes. J Biol Chem (2012) 0.87

Hsp90 structure: when two ends meet. Nat Struct Mol Biol (2006) 0.86

Hsp33 controls elongation factor-Tu stability and allows Escherichia coli growth in the absence of the major DnaK and trigger factor chaperones. J Biol Chem (2012) 0.86

Structure and function of Hip, an attenuator of the Hsp70 chaperone cycle. Nat Struct Mol Biol (2013) 0.86

Lon protease quality control of presecretory proteins in Escherichia coli and its dependence on the SecB and DnaJ (Hsp40) chaperones. J Biol Chem (2010) 0.86