grpE

Summary

Gene Symbol: grpE
Description: heat shock protein
Alias: ECK2610, JW2594
Species: Escherichia coli str. K-12 substr. MG1655
Products:     grpE

Top Publications

  1. Liberek K, Marszalek J, Ang D, Georgopoulos C, Zylicz M. Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc Natl Acad Sci U S A. 1991;88:2874-8 pubmed
    The products of the Escherichia coli dnaK, dnaJ, and grpE heat shock genes have been previously shown to be essential for bacteriophage lambda DNA replication at all temperatures and for bacterial survival under certain conditions...
  2. Yoshimune K, Yoshimura T, Nakayama T, Nishino T, Esaki N. Hsc62, Hsc56, and GrpE, the third Hsp70 chaperone system of Escherichia coli. Biochem Biophys Res Commun. 2002;293:1389-95 pubmed
    ..b>GrpE, a nucleotide exchange factor for DnaK, also stimulated the ATPase activity of Hsc62 in the presence of Hsc56...
  3. Doyle S, Shastry S, Kravats A, Shih Y, Miot M, Hoskins J, et al. Interplay between E. coli DnaK, ClpB and GrpE during protein disaggregation. J Mol Biol. 2015;427:312-27 pubmed publisher
    ..subdomain IIB mutants were also defective in the ability to disaggregate protein aggregates with ClpB, DnaJ and GrpE, although they retained some ability to reactivate proteins with DnaJ and GrpE in the absence of ClpB...
  4. Mehl A, Okada K, Dehn S, Kurian S. Probing the stability and mechanism for folding of the GrpE1-112 tetrameric deletion mutant of the GrpE protein from E. coli. Biochem Biophys Res Commun. 2012;420:635-8 pubmed publisher
    ..A deletion mutant of the GrpE protein from Escherichia coli, that contains the first 112 residues (GrpE1-112) of 197 total, is an oligomeric ..
  5. Zhang Y, Griffiths M. Induced expression of the heat shock protein genes uspA and grpE during starvation at low temperatures and their influence on thermal resistance of Escherichia coli O157:H7. J Food Prot. 2003;66:2045-50 pubmed
    ..In this study, the promoters for two genes encoding heat shock proteins involved in many stress responses, UspA and GrpE, were fused with the green fluorescent protein (gfp) gene...
  6. Wu B, Wawrzynow A, Zylicz M, Georgopoulos C. Structure-function analysis of the Escherichia coli GrpE heat shock protein. EMBO J. 1996;15:4806-16 pubmed
    We have isolated various missense mutations in the essential grpE gene of Escherichia coli based on the inability to propagate bacteriophage lambda...
  7. Siegenthaler R, Grimshaw J, Christen P. Immediate response of the DnaK molecular chaperone system to heat shock. FEBS Lett. 2004;562:105-10 pubmed
    ..In recent experiments with the Hsp70 system of Escherichia coli, the co-chaperone GrpE has been found to undergo a reversible thermal transition in the physiological temperature range...
  8. Gelinas A, Langsetmo K, Toth J, Bethoney K, Stafford W, Harrison C. A structure-based interpretation of E.coli GrpE thermodynamic properties. J Mol Biol. 2002;323:131-42 pubmed
    b>GrpE is the nucleotide exchange factor for the Escherichia coli molecular chaperone DnaK, the prokaryotic homologue of Hsp70...
  9. Johnson C, Chandrasekhar G, Georgopoulos C. Escherichia coli DnaK and GrpE heat shock proteins interact both in vivo and in vitro. J Bacteriol. 1989;171:1590-6 pubmed
    Previous studies have demonstrated that the Escherichia coli dnaK and grpE genes code for heat shock proteins. Both the Dnak and GrpE proteins are necessary for bacteriophage lambda DNA replication and for E...

More Information

Publications68

  1. Sugimoto S, Higashi C, Saruwatari K, Nakayama J, Sonomoto K. A gram-negative characteristic segment in Escherichia coli DnaK is essential for the ATP-dependent cooperative function with the co-chaperones DnaJ and GrpE. FEBS Lett. 2007;581:2993-9 pubmed
    ..that a segment-deletion mutant DnaKDelta74-96 became defective in the cooperation with the co-chaperones DnaJ and GrpE. In addition, in vivo complementation assay showed that expression of DnaKDelta74-96 could not rescue the viability ..
  2. Fredriksson A, Ballesteros M, Dukan S, Nystrom T. Defense against protein carbonylation by DnaK/DnaJ and proteases of the heat shock regulon. J Bacteriol. 2005;187:4207-13 pubmed
  3. Zzaman S, Reddy J, Bastia D. The DnaK-DnaJ-GrpE chaperone system activates inert wild type pi initiator protein of R6K into a form active in replication initiation. J Biol Chem. 2004;279:50886-94 pubmed
    ..Here we show that the chaperone DnaK along with its co-chaperone DnaJ and the nucleotide exchange factor GrpE were needed to activate WT pi and caused it to initiate replication in vitro at the correct origin...
  4. Lipinska B, King J, Ang D, Georgopoulos C. Sequence analysis and transcriptional regulation of the Escherichia coli grpE gene, encoding a heat shock protein. Nucleic Acids Res. 1988;16:7545-62 pubmed
    We have sequenced the Escherichia coli grpE gene and shown that it encodes a 197-amino acid residue protein of 21,668-Mr...
  5. Nian R, Tan L, Yoo I, Choe W. Chaperone-assisted column refolding of gloshedobin with the use of refolding cocktail. J Chromatogr A. 2008;1214:47-58 pubmed publisher
    ..In this study, a new refolding strategy harnessing the ClpB and DnaK/DnaJ/GrpE bichaperone system is demonstrated to be superior to the conventional refolding methods in either batch dilution or ..
  6. Hu B, Tomita M. The Hsp70 chaperone system maintains high concentrations of active proteins and suppresses ATP consumption during heat shock. Syst Synth Biol. 2007;1:47-58 pubmed publisher
    ..The reverse transition from the R state to the T state is accelerated by the nucleotide exchange factor GrpE. These two processes, T-to-R and R-to-T conversion, are affected differently by temperature change...
  7. Zhu X, Zhao X, Burkholder W, Gragerov A, Ogata C, Gottesman M, et al. Structural analysis of substrate binding by the molecular chaperone DnaK. Science. 1996;272:1606-14 pubmed
    ..This domain is rotated in the molecules of a second crystal lattice, which suggests a model of conformation-dependent substrate binding that features a latch mechanism for maintaining long lifetime complexes. ..
  8. Skowyra D, Wickner S. GrpE alters the affinity of DnaK for ATP and Mg2+. Implications for the mechanism of nucleotide exchange. J Biol Chem. 1995;270:26282-5 pubmed
    DnaK, DnaJ, and GrpE heat shock proteins of Escherichia coli activate site-specific DNA binding by the RepA replication initiator protein of plasmid P1 in a reaction dependent on ATP and Mg2+...
  9. Sugimoto S, Saruwatari K, Higashi C, Sonomoto K. The proper ratio of GrpE to DnaK is important for protein quality control by the DnaK-DnaJ-GrpE chaperone system and for cell division. Microbiology. 2008;154:1876-85 pubmed publisher
    ..Here, the physiological consequences of overexpression of GrpE in wild-type Escherichia coli MC4100 were examined...
  10. Wickner S, Skowyra D, Hoskins J, McKenney K. DnaJ, DnaK, and GrpE heat shock proteins are required in oriP1 DNA replication solely at the RepA monomerization step. Proc Natl Acad Sci U S A. 1992;89:10345-9 pubmed
    We have found that three Escherichia coli heat shock proteins, DnaK (the hsp70 homolog), DnaJ, and GrpE, function in oriP1 DNA replication in vitro solely to activate DNA binding by the replication initiator protein RepA...
  11. Siegenthaler R, Christen P. The importance of having thermosensor control in the DnaK chaperone system. J Biol Chem. 2005;280:14395-401 pubmed
    In addition to the sigma(32)-mediated heat shock response, the DnaK/DnaJ/GrpE molecular chaperone system of Escherichia coli directly adapts to elevated temperatures by sequestering a higher fraction of substrate...
  12. Melero R, Moro F, Pérez Calvo M, Perales Calvo J, Quintana Gallardo L, Llorca O, et al. Modulation of the chaperone DnaK allosterism by the nucleotide exchange factor GrpE. J Biol Chem. 2015;290:10083-92 pubmed publisher
    ..the Hsp40 co-chaperones (DnaJ in Escherichia coli) induce the ADP state, and the nucleotide exchange factors (GrpE in E. coli) induce the ATP state...
  13. Zmijewski M, Kwiatkowska J, Lipinska B. Complementation studies of the DnaK-DnaJ-GrpE chaperone machineries from Vibrio harveyi and Escherichia coli, both in vivo and in vitro. Arch Microbiol. 2004;182:436-49 pubmed
    ..The DnaK-DnaJ-GrpE chaperone machinery of V...
  14. Harrison C. GrpE, a nucleotide exchange factor for DnaK. Cell Stress Chaperones. 2003;8:218-24 pubmed
    The cochaperone GrpE functions as a nucleotide exchange factor to promote dissociation of adenosine 5'-diphosphate (ADP) from the nucleotide-binding cleft of DnaK...
  15. Brehmer D, Gässler C, Rist W, Mayer M, Bukau B. Influence of GrpE on DnaK-substrate interactions. J Biol Chem. 2004;279:27957-64 pubmed
    ..This interaction is regulated by the DnaJ and GrpE co-chaperones, which stimulate ATP hydrolysis and nucleotide exchange by DnaK, respectively...
  16. Gamer J, Bujard H, Bukau B. Physical interaction between heat shock proteins DnaK, DnaJ, and GrpE and the bacterial heat shock transcription factor sigma 32. Cell. 1992;69:833-42 pubmed
    ..This report presents evidence for the physical association of DnaK, DnaJ, and GrpE chaperones with sigma 32 in vivo...
  17. Ha J, McKay D. Kinetics of nucleotide-induced changes in the tryptophan fluorescence of the molecular chaperone Hsc70 and its subfragments suggest the ATP-induced conformational change follows initial ATP binding. Biochemistry. 1995;34:11635-44 pubmed
    ..The 44 kDa ATPase fragment does not show biphasic kinetics for ATP binding, and does not show fluorescence changes that suggest conformational changes of the type seen in Hsc70 and the 60 kDa fragment. ..
  18. Ang D, Georgopoulos C. The heat-shock-regulated grpE gene of Escherichia coli is required for bacterial growth at all temperatures but is dispensable in certain mutant backgrounds. J Bacteriol. 1989;171:2748-55 pubmed
    Previous work has established that the grpE+ gene product is a heat shock protein that is essential for bacteriophage lambda growth at all temperatures and for Escherichia coli growth at temperatures above 43 degrees C...
  19. Mehl A, Demeler B, Zraikat A. A water mediated electrostatic interaction gives thermal stability to the "tail" region of the GrpE protein from E. coli. Protein J. 2007;26:239-45 pubmed
    The GrpE protein from E. coli is a homodimer with an unusual structure of two long paired alpha-helices from each monomer interacting in a parallel arrangement to form a "tail" at the N-terminal end...
  20. Kerner M, Naylor D, Ishihama Y, Maier T, Chang H, Stines A, et al. Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli. Cell. 2005;122:209-20 pubmed
    ..We suggest that the chaperonin system may have facilitated the evolution of this fold into a versatile platform for the implementation of numerous enzymatic functions. ..
  21. Kluck C, Patzelt H, Genevaux P, Brehmer D, Rist W, Schneider Mergener J, et al. Structure-function analysis of HscC, the Escherichia coli member of a novel subfamily of specialized Hsp70 chaperones. J Biol Chem. 2002;277:41060-9 pubmed
    ..The HscC ATPase was not affected by the nucleotide exchange factor of DnaK GrpE and stimulated 8-fold by DjlC, a DnaJ protein with a putative transmembrane domain, but not by other DnaJ proteins ..
  22. Moro F, Taneva S, Velazquez Campoy A, Muga A. GrpE N-terminal domain contributes to the interaction with Dnak and modulates the dynamics of the chaperone substrate binding domain. J Mol Biol. 2007;374:1054-64 pubmed
    b>GrpE acts as a nucleotide exchange factor for DnaK, the main Hsp70 protein in bacteria, accelerating ADP/ATP exchange by several orders of magnitude...
  23. Harrison C, Hayer Hartl M, Di Liberto M, Hartl F, Kuriyan J. Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Science. 1997;276:431-5 pubmed
    The crystal structure of the adenine nucleotide exchange factor GrpE in complex with the adenosine triphosphatase (ATPase) domain of Escherichia coli DnaK [heat shock protein 70 (Hsp70)] was determined at 2.8 angstrom resolution...
  24. Mehl A, Heskett L, Jain S, Demeler B. Insights into dimerization and four-helix bundle formation found by dissection of the dimer interface of the GrpE protein from Escherichia coli. Protein Sci. 2003;12:1205-15 pubmed
    The GrpE heat shock protein from Escherichia coli has a homodimeric structure...
  25. Wall D, Zylicz M, Georgopoulos C. The NH2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for lambda replication. J Biol Chem. 1994;269:5446-51 pubmed
    ..These results may be applicable to other eukaryotic proteins that contain this conserved J domain as proteins that interact and stimulate the hydrolysis of ATP by their cognate HSP70 proteins...
  26. Mogk A, Deuerling E, Vorderwülbecke S, Vierling E, Bukau B. Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation. Mol Microbiol. 2003;50:585-95 pubmed
    ..The DnaK requirement for growth is increasingly higher for delta ibpAB, delta clpB, and the double delta ibpAB delta clpB mutant cells, establishing the positions of sHsps and ClpB in this chaperone triade. ..
  27. Zietkiewicz S, Krzewska J, Liberek K. Successive and synergistic action of the Hsp70 and Hsp100 chaperones in protein disaggregation. J Biol Chem. 2004;279:44376-83 pubmed
    ..Bacterial Hsp70 (DnaK), its co-chaperones (DnaJ and GrpE), and Hsp100 (ClpB) were incubated with aggregated GFP, and the increase in GFP fluorescence was monitored...
  28. Fredriksson A, Nystrom T. Conditional and replicative senescence in Escherichia coli. Curr Opin Microbiol. 2006;9:612-8 pubmed
    ..Thus, bacterial physiology might entail both conditional and mandatory aging processes. ..
  29. Laskowska E, Bohdanowicz J, Kuczynska Wisnik D, Matuszewska E, Kedzierska S, Taylor A. Aggregation of heat-shock-denatured, endogenous proteins and distribution of the IbpA/B and Fda marker-proteins in Escherichia coli WT and grpE280 cells. Microbiology. 2004;150:247-59 pubmed
    ..normally never found in the outer-membrane (OM) fraction of WT cells, were present in the OM fraction from grpE cells after heat shock...
  30. Thomas J, Baneyx F. ClpB and HtpG facilitate de novo protein folding in stressed Escherichia coli cells. Mol Microbiol. 2000;36:1360-70 pubmed
    DnaK-DnaJ-GrpE and GroEL-GroES are the best-characterized molecular chaperone systems in the cytoplasm of Escherichia coli...
  31. Liu C, Perrett S, Zhou J. Dimeric trigger factor stably binds folding-competent intermediates and cooperates with the DnaK-DnaJ-GrpE chaperone system to allow refolding. J Biol Chem. 2005;280:13315-20 pubmed
    ..glyceraldehyde-3-phosphate dehydrogenase (GAPDH) reactivation yield in the presence and absence of the DnaK-DnaJ-GrpE chaperone system in vitro...
  32. Nunes J, Mayer Hartl M, Hartl F, Müller D. Action of the Hsp70 chaperone system observed with single proteins. Nat Commun. 2015;6:6307 pubmed publisher
    ..DnaJ accelerates ATP hydrolysis on DnaK, by closing the peptide-binding cleft of DnaK. GrpE catalysed nucleotide exchange and ATP re-binding then lead to substrate release from DnaK, allowing folding...
  33. Gelinas A, Toth J, Bethoney K, Langsetmo K, Stafford W, Harrison C. Thermodynamic linkage in the GrpE nucleotide exchange factor, a molecular thermosensor. Biochemistry. 2003;42:9050-9 pubmed
    b>GrpE is the nucleotide exchange factor for the Escherichia coli molecular chaperone DnaK, the bacterial homologue of Hsp70...
  34. Grimshaw J, Siegenthaler R, Züger S, Schönfeld H, Z graggen B, Christen P. The heat-sensitive Escherichia coli grpE280 phenotype: impaired interaction of GrpE(G122D) with DnaK. J Mol Biol. 2005;353:888-96 pubmed
    b>GrpE is the nucleotide-exchange factor of the DnaK chaperone system...
  35. Grimshaw J, Jelesarov I, Schönfeld H, Christen P. Reversible thermal transition in GrpE, the nucleotide exchange factor of the DnaK heat-shock system. J Biol Chem. 2001;276:6098-104 pubmed
    DnaK, a Hsp70 acting in concert with its co-chaperones DnaJ and GrpE, is essential for Escherichia coli to survive environmental stress, including exposure to elevated temperatures...
  36. Shi W, Zhou Y, Wild J, Adler J, Gross C. DnaK, DnaJ, and GrpE are required for flagellum synthesis in Escherichia coli. J Bacteriol. 1992;174:6256-63 pubmed
    The DnaK, DnaJ, and GrpE heat shock proteins are required for motility of Escherichia coli...
  37. Goloubinoff P, Mogk A, Zvi A, Tomoyasu T, Bukau B. Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Proc Natl Acad Sci U S A. 1999;96:13732-7 pubmed
    ..We show here that the sequential action of two Escherichia coli chaperone systems, ClpB and DnaK-DnaJ-GrpE, can efficiently solubilize excess amounts of protein aggregates and refold them into active proteins...
  38. Nam S, Walsh M. Characterization of interactions between Escherichia coli molecular chaperones and immobilized caseins. Prep Biochem Biotechnol. 2003;33:321-39 pubmed
    ..Western analysis identified five E. coli molecular chaperones including DnaK, DnaJ, GrpE, GroEL, and GroES in eluates...
  39. Reidy M, Miot M, Masison D. Prokaryotic chaperones support yeast prions and thermotolerance and define disaggregation machinery interactions. Genetics. 2012;192:185-93 pubmed publisher
    ..Our results define cooperative interactions among these components that are specific or interchangeable across life kingdoms and imply Hsp100 family disaggregases possess intrinsic amyloid remodeling activity. ..
  40. de Marco A. Protocol for preparing proteins with improved solubility by co-expressing with molecular chaperones in Escherichia coli. Nat Protoc. 2007;2:2632-9 pubmed
    Eight combinations of molecular chaperones (e.g., DnaK/DnaJ/GrpE/ClpB) are co-expressed with the target recombinant protein to compare their effectiveness in improving its soluble yield...
  41. Barnett M, Nagy M, Kedzierska S, Zolkiewski M. The amino-terminal domain of ClpB supports binding to strongly aggregated proteins. J Biol Chem. 2005;280:34940-5 pubmed
    ..dehydrogenase (G6PDH) by ClpB and its N-terminally truncated variant ClpBDeltaN in the presence of DnaK, DnaJ, and GrpE. We found that the chaperone activity of ClpBDeltaN becomes significantly lower than that of the full-length ClpB ..
  42. Houry W. Chaperone-assisted protein folding in the cell cytoplasm. Curr Protein Pept Sci. 2001;2:227-44 pubmed
    ..2) The Hsp 70 system consisting of DnaK (Hsp 70), its cofactor DnaJ (Hsp 40), and the nucleotide exchange factor GrpE. This system recognizes polypeptide chains in an extended conformation...
  43. Konieczny I, Liberek K. Cooperative action of Escherichia coli ClpB protein and DnaK chaperone in the activation of a replication initiation protein. J Biol Chem. 2002;277:18483-8 pubmed
    ..In this work we demonstrate that the combined action of ClpB and the DnaK, DnaJ, and GrpE chaperones leads to the activation of DNA replication of the broad-host-range plasmid RK2...
  44. Ying B, Taguchi H, Ueda H, Ueda T. Chaperone-assisted folding of a single-chain antibody in a reconstituted translation system. Biochem Biophys Res Commun. 2004;320:1359-64 pubmed
    ..In addition, both systems also acted as chaperones after translation had been stopped. In contrast, the GroEL/ES system showed little or no co- or post-translational assistance in folding. ..
  45. Chow I, Barnett M, Zolkiewski M, Baneyx F. The N-terminal domain of Escherichia coli ClpB enhances chaperone function. FEBS Lett. 2005;579:4242-8 pubmed
    ..Our results are consistent with a model in which the N-domain of ClpB95 maximizes substrate processing under conditions where the cellular supply of free DnaK-DnaJ is limiting. ..
  46. Bukau B, Horwich A. The Hsp70 and Hsp60 chaperone machines. Cell. 1998;92:351-66 pubmed
  47. Straus D, Walter W, Gross C. DnaK, DnaJ, and GrpE heat shock proteins negatively regulate heat shock gene expression by controlling the synthesis and stability of sigma 32. Genes Dev. 1990;4:2202-9 pubmed
    ..coli heat shock gene expression. We report that two other heat shock proteins, DnaJ and GrpE, are also involved in the negative regulation of heat shock gene expression...
  48. Wu B, Ang D, Snavely M, Georgopoulos C. Isolation and characterization of point mutations in the Escherichia coli grpE heat shock gene. J Bacteriol. 1994;176:6965-73 pubmed
    The Escherichia coli grpE gene (along with dnaK, dnaJ, groEL, and groES) was originally identified as one of the host factors required for phage lambda growth...
  49. Han W, Christen P. Interdomain communication in the molecular chaperone DnaK. Biochem J. 2003;369:627-34 pubmed
    ..fluorescence of DnaK offer a simple means not only to follow the binding of ATP and of ADP plus the co-chaperone GrpE to the ATPase domain, but also to investigate the kinetics of peptide binding to the substrate-binding domain of ..
  50. Maki J, Schnobrich D, Culver G. The DnaK chaperone system facilitates 30S ribosomal subunit assembly. Mol Cell. 2002;10:129-38 pubmed
    ..Purified DnaK, its cochaperones DnaJ and GrpE, and ATP can facilitate reconstitution of functional 30S subunits under otherwise nonpermissive conditions...
  51. Kim Y, Min J, Hong H, Park J, Park K, Gu M. Gene expression analysis and classification of mode of toxicity of polycyclic aromatic hydrocarbons (PAHs) in Escherichia coli. Chemosphere. 2007;66:1243-8 pubmed
    ..In this study, therefore, the expression of recA, katG, fabA and grpE genes was used as a representative for DNA, oxidative, membrane and protein damage, respectively, after E...
  52. Kedzierska S, Matuszewska E. The effect of co-overproduction of DnaK/DnaJ/GrpE and ClpB proteins on the removal of heat-aggregated proteins from Escherichia coli DeltaclpB mutant cells--new insight into the role of Hsp70 in a functional cooperation with Hsp100. FEMS Microbiol Lett. 2001;204:355-60 pubmed
    The effect of overproduction of the Hsp70 system proteins (DnaK, DnaJ, GrpE) and/or ClpB (Hsp100) from plasmids on the process of formation and removal of heat-aggregated proteins from Escherichia coli cells (the S fraction) was ..
  53. Zolkiewski M. ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli. J Biol Chem. 1999;274:28083-6 pubmed
    ..Conventional chaperone systems (GroEL/GroES and DnaK/DnaJ/GrpE) or ClpB alone did not reactivate luciferase under those conditions...
  54. Ishiai M, Wada C, Kawasaki Y, Yura T. Mini-F plasmid mutants able to replicate in Escherichia coli deficient in the DnaJ heat shock protein. J Bacteriol. 1992;174:5597-603 pubmed
    A subset of Escherichia coli heat shock proteins, DnaJ, DnaK, and GrpE, is required for mini-F plasmid replication, presumably at the step of functioning of the RepE initiator protein...
  55. Grimshaw J, Jelesarov I, Siegenthaler R, Christen P. Thermosensor action of GrpE. The DnaK chaperone system at heat shock temperatures. J Biol Chem. 2003;278:19048-53 pubmed
    Temperature directly controls functional properties of the DnaK/DnaJ/GrpE chaperone system...
  56. Saito M, Tsugawa A, Egawa K, Nakamura Y. Revised sequence of the nusA gene of Escherichia coli and identification of nusA11 (ts) and nusA1 mutations which cause changes in a hydrophobic amino acid cluster. Mol Gen Genet. 1986;205:380-2 pubmed
    ..In the course of these experiments, several mistakes in the published nusA nucleotide sequence were found. These errors are revised in this article. The molecular weight of NusA is accordingly revised to 54,430. ..
  57. Gamer J, Multhaup G, Tomoyasu T, McCarty J, Rudiger S, Schönfeld H, et al. A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32. EMBO J. 1996;15:607-17 pubmed
    The chaperone system formed by DnaK, DnaJ and GrpE mediates stress-dependent negative modulation of the Escherichia coli heat shock response, probably through association with the heat shock promoter-specific sigma32 subunit of RNA ..
  58. Sugimoto S, Higashi C, Yoshida H, Sonomoto K. Construction of Escherichia coli dnaK-deletion mutant infected by lambdaDE3 for overexpression and purification of recombinant GrpE proteins. Protein Expr Purif. 2008;60:31-6 pubmed publisher
    ..Using this host cell, recombinant hexa histidine-tag fused GrpE, which is well known as a co-chaperone for DnaK and to strongly interact with DnaK, was overexpressed and purified ..
  59. Saito H, Uchida H. Initiation of the DNA replication of bacteriophage lambda in Escherichia coli K12. J Mol Biol. 1977;113:1-25 pubmed