-
1
-
-
0001934012
-
Expression of proteins in bacteria
-
Edited by Cleland JL, Craik CS. New York: Butterworths
-
Georgiou G: Expression of proteins in bacteria. In Principles and Practice of Protein Engineering. Edited by Cleland JL, Craik CS. New York: Butterworths; 1995:101-127. An overview of recombinant protein expression in bacteria. Problems relating to transcription, translation, proteolysis, inclusion body formation and cell growth are discussed.
-
(1995)
Principles and Practice of Protein Engineering.
, pp. 101-127
-
-
Georgiou, G.1
-
2
-
-
0028533566
-
Recent developments in heterologous protein production
-
Hockney RC: Recent developments in heterologous protein production in Escherichia coli. Trends Biotechnol 1994, 12:456-463. A recent review describing various strategies for the expression of active recombinant proteins in E. coli.
-
(1994)
Escherichia Coli. Trends Biotechnol
, vol.12
, pp. 456-463
-
-
Hockney, R.C.1
-
3
-
-
0028402689
-
The barriers in protein folding
-
Sosnick TR, Mayne L, Hiller R, Englander SW: The barriers in protein folding. Struct Biol 1994, 1:149-156. This article shows that cytochrome c folds extremely rapidly (in the 10ms range). In contrast to other current views on the mechanism of protein folding, the data in this paper argue against the formation of the 'obligatory' intermediate in the folding pathway.
-
(1994)
Struct Biol
, vol.1
, pp. 149-156
-
-
Sosnick, T.R.1
Mayne, L.2
Hiller, R.3
Englander, S.W.4
-
4
-
-
0028298127
-
Mutations and off-pathway aggregation of proteins
-
Wetzel R: Mutations and off-pathway aggregation of proteins. Trends Biotechnol 1994, 12:193-198. A review of protein aggregation in vivo with special emphasis on the effect of amino acid substitutions on the self-association of folding intermediates.
-
(1994)
Trends Biotechnol
, vol.12
, pp. 193-198
-
-
Wetzel, R.1
-
5
-
-
0028559525
-
Folding and aggregation of TEM β-lactamase: Analogies with the formation of inclusion bodies in Escherichia coli
-
Georgiou G, Valax P, Ostermeier M, Horowitz PM: Folding and aggregation of TEM β-lactamase: analogies with the formation of inclusion bodies in Escherichia coli. Protein Sci 1994, 3:1953-1960. In vitro studies of β-lactamase folding show that an intermediate with the characteristics of a molten globule is populated at intermediate denaturant concentration. This intermediate is prone to aggregation. Conditions such as the addition of sucrose, lower temperatures and the absence of reducing agents are demonstrated to prevent protein aggregation in vitro and correlate well with observations in vivo on inclusion body formation.
-
(1994)
Protein Sci
, vol.3
, pp. 1953-1960
-
-
Georgiou, G.1
Valax, P.2
Ostermeier, M.3
Horowitz, P.M.4
-
6
-
-
0028117314
-
Molecular chaperones in protein folding: The art of avoiding sticky situations
-
Hartl FU, Hlodan R, Langer T: Molecular chaperones in protein folding: the art of avoiding sticky situations. Trends Biochem Sci 1994, 19:20-25. Review on the role of chaperones in the intracellular folding and aggregation.
-
(1994)
Trends Biochem Sci
, vol.19
, pp. 20-25
-
-
Hartl, F.U.1
Hlodan, R.2
Langer, T.3
-
7
-
-
0029000134
-
The ClpX heat shock protein of E. coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone
-
Wawrzynow A, Wojtkowiak D, Marszalek J, Banecki B, Jonsen M, Graves B, Georgopoulos C, Zylicz M: The ClpX heat shock protein of E. coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone. EMBO J 1995, 14:1867-1877. ClpX mediates the degradation of the bacteriophage λO replication protein by ClpP. This paper shows that, in the absence of ClpP, ClpX exhibits the properties of a molecular chaperone, including the protection of λO from thermally induced aggregation and the disaggregation of associated λO. These activities depend on the presence of ATP or its non-hydrolyzable analog ATP-λ-S.
-
(1995)
EMBO J
, vol.14
, pp. 1867-1877
-
-
Wawrzynow, A.1
Wojtkowiak, D.2
Marszalek, J.3
Banecki, B.4
Jonsen, M.5
Graves, B.6
Georgopoulos, C.7
Zylicz, M.8
-
8
-
-
0027996745
-
A molecular chaperone, ClpA, functions like DnaK and DnaJ
-
Wickner S, Gottesman S, Skwyra D, Hoskins J, MacKenney K, Maurizi M: A molecular chaperone, ClpA, functions like DnaK and DnaJ. Proc Natl Acad Sci USA 1994, 91:1221B-12222. It is shown that ClpA is an ATP-dependent molecular chaperone that both functions like DnaK/J during the in vitro activation of RepA and protects luciferase against heat inactivation.
-
(1994)
Proc Natl Acad Sci USA
, vol.91
-
-
Wickner, S.1
Gottesman, S.2
Skwyra, D.3
Hoskins, J.4
MacKenney, K.5
Maurizi, M.6
-
9
-
-
0024578552
-
GroE heat shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli
-
Goloubinoff P, Gatenby AA, Lorimer GH: GroE heat shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli. Nature 1989, 337:44-47.
-
(1989)
Nature
, vol.337
, pp. 44-47
-
-
Goloubinoff, P.1
Gatenby, A.A.2
Lorimer, G.H.3
-
10
-
-
0029114645
-
High level expression of functional rat neuronal nitric oxide synthase in Escherichia coli
-
-1. In the absence of molecular chaperones, expression of nNOS is either very low or undetectable, depending on the E. coli strain used The nNOS produced in this system is shown to be indistinguishable from nNOS expressed in human kidney 293 cells.
-
(1995)
Proc Natl Acad Sci USA
, vol.92
, pp. 8428-8432
-
-
Roman, L.J.1
Sheta, E.A.2
Martasek, P.3
Gross, S.S.4
Liu, O.5
Silver-Masters, B.S.6
-
11
-
-
0027861114
-
Molecular cloning and expression of the catalytic subunit of bovine pyruvate dehydrogenase phosphatase and sequence similarity with protein phosphatase 2C
-
Lawson JE, Niu X-D, Browning KS, Le Trong H, Yan J, Reed LJ: Molecular cloning and expression of the catalytic subunit of bovine pyruvate dehydrogenase phosphatase and sequence similarity with protein phosphatase 2C. Biochemistry 1993, 32:8987-8993.
-
(1993)
Biochemistry
, vol.32
, pp. 8987-8993
-
-
Lawson, J.E.1
Niu, X.-D.2
Browning, K.S.3
Le Trong, H.4
Yan, J.5
Reed, L.J.6
-
12
-
-
0026726710
-
Effect of overproduction of heat shock chaperones GrbESL and DnaK on human procollagenase production in Escherichia coli
-
Lee SC, Olins PO: Effect of overproduction of heat shock chaperones GrbESL and DnaK on human procollagenase production in Escherichia coli. J Biol Chem 1992, 267:2849-2852.
-
(1992)
J Biol Chem
, vol.267
, pp. 2849-2852
-
-
Lee, S.C.1
Olins, P.O.2
-
13
-
-
0026568947
-
DnaK-mediated alterations in human growth hormone protein inclusion bodies
-
Blum P, Velligan M, Lin N, Matin A: DnaK-mediated alterations in human growth hormone protein inclusion bodies. Biotechnology 1992, 10:301-304.
-
(1992)
Biotechnology
, vol.10
, pp. 301-304
-
-
Blum, P.1
Velligan, M.2
Lin, N.3
Matin, A.4
-
14
-
-
0028988858
-
DnaK/DnaJ supplementation improves the periplasmic production of human granulocyte-colony stimulating factor in Escherichia coli
-
Pérez-Pérez J, Matinez-Caja C, Barbero JL: DnaK/DnaJ supplementation improves the periplasmic production of human granulocyte-colony stimulating factor in Escherichia coli. Biochem Biophys Res Comm 1995, 210:524-529. Human granulocyte colony-stimulating factor is expressed in E. coli as a fusion to a chimeric signal peptide. Supplementing the host with DnaK/J proteins improves the secretion of the recombinant protein. This paper demonstrates that the improvement in secretion can be attributed to an increase in the solubility of the precursor protein in the cytoplasm.
-
(1995)
Biochem Biophys Res Comm
, vol.210
, pp. 524-529
-
-
Pérez-Pérez, J.1
Matinez-Caja, C.2
Barbero, J.L.3
-
15
-
-
0025375220
-
Heat shock proteins DnaK and GroEL facilitate the export of LacZ hybrid proteins in E. coli
-
Philips GJ, Silhavy TJ: Heat shock proteins DnaK and GroEL facilitate the export of LacZ hybrid proteins in E. coli. Nature 1990, 344:882-884.
-
(1990)
Nature
, vol.344
, pp. 882-884
-
-
Philips, G.J.1
Silhavy, T.J.2
-
16
-
-
0027744759
-
Co-expression of plastid chaperonin genes and a synthetic plant Rubisco operon in Escherichia coli
-
Cloney LP, Bekkaoui DR, Hemmingsen SM: Co-expression of plastid chaperonin genes and a synthetic plant Rubisco operon in Escherichia coli. Plant Mol Biol 1993, 23:1285-1290.
-
(1993)
Plant Mol Biol
, vol.23
, pp. 1285-1290
-
-
Cloney, L.P.1
Bekkaoui, D.R.2
Hemmingsen, S.M.3
-
17
-
-
0026498778
-
Physiological consequences of DnaK and DnaJ overproduction in Escherichia coli
-
Blum P, Ory J, Bauernfeind J, Krska J: Physiological consequences of DnaK and DnaJ overproduction in Escherichia coli. J Bacteriol 1994, 174:7436-7444. The influence of various levels of expression of the DnaK/J proteins on the physiology of E. coli cells is evaluated. The effects range from plasmid instability to defects in cell septation, filamentation and cell death, depending on the level of DnaK expression.
-
(1994)
J Bacteriol
, vol.174
, pp. 7436-7444
-
-
Blum, P.1
Ory, J.2
Bauernfeind, J.3
Krska, J.4
-
18
-
-
14744269790
-
Structure and morphology of inclusion bodies in Escherichia coli
-
Bowden GA, Paredes AM, Georgiou G: Structure and morphology of inclusion bodies in Escherichia coli. Biotechnology 1991, 9:725-730.
-
(1991)
Biotechnology
, vol.9
, pp. 725-730
-
-
Bowden, G.A.1
Paredes, A.M.2
Georgiou, G.3
-
19
-
-
0027997012
-
Correctly folded T-cell receptor fragments in the periplasm of Escherichia coli. Influence of folding catalysts
-
Wulfing C, Plückthun A: Correctly folded T-cell receptor fragments in the periplasm of Escherichia coli. Influence of folding catalysts. J Mol Biol 1994, 242:655-669. This paper describes a systematic study of chaperone or foldase overexpression and growth condition optimization to achieve the production of soluble single-chain T-cell receptors in the periplasmic space of E. coli. Optimal production is obtained in cells co-expressing DsbA and RpoH, the sigma factor responsible for the transcription of most heat-shock proteins. A model for the folding of single-chain T-cell receptors in the periplasmic space is presented.
-
(1994)
J Mol Biol
, vol.242
, pp. 655-669
-
-
Wulfing, C.1
Plückthun, A.2
-
20
-
-
0028286019
-
Protein folding in the periplasm of Escherichia coli
-
Wulfing C, Plückthun A: Protein folding in the periplasm of Escherichia coli. Mol Microbiol 1994, 12:685-692. Review detailing the mechanism of protein folding in the periplasm in E. coli and the interactions of secreted proteins with periplasmic foldases.
-
(1994)
Mol Microbiol
, vol.12
, pp. 685-692
-
-
Wulfing, C.1
Plückthun, A.2
-
21
-
-
0028028387
-
Building bridges: Disulphide bond formation in the cell
-
Bardwell JCA: Building bridges: disulphide bond formation in the cell. Mol Microbiol 1994, 14:199-205. This review offers a description of the Dsb periplasmic disulfide bond formation machinery of E. coli.
-
(1994)
Mol Microbiol
, vol.14
, pp. 199-205
-
-
Jca, B.1
-
22
-
-
0028809455
-
Characterization of an Escherichia coli rotA mutant affected in periplasmic peptidylprolyl cis/trans isomerase
-
Kleerebezem M, Heutink M, Tommassen J: Characterization of an Escherichia coli rotA mutant affected in periplasmic peptidylprolyl cis/trans isomerase. Mol Microbiol 1995, 18:313-320. In this paper, a mutant with a chromosomal deletion in the periplasmic peptidylproline isomerase rotA gene is create. It is shown that rotA does not confer a detectable phenotype and is not important for the folding of secreted proteins.
-
(1995)
Mol Microbiol
, vol.18
, pp. 313-320
-
-
Kleerebezem, M.1
Heutink, M.2
Tommassen, J.3
-
23
-
-
0028296940
-
The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation
-
Missiakas D, Georgopoulos C, Raina S: The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulfide bond formation. EMBO J 1994, 13:2013-2020. In this article, the dsbC gene product is identified and ils function characterized. DsbC is overexpressed, purified and shown to have an activity similar to that of DsbA in the dithiothreitol-dependent reduction of insulin in vitro.
-
(1994)
EMBO J
, vol.13
, pp. 2013-2020
-
-
Missiakas, D.1
Georgopoulos, C.2
Raina, S.3
-
24
-
-
0028979629
-
Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli
-
Missiakas D, Schwager F, Raina S: Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli. EMBO J 1995, 14:3415-3424. A gene encoding a new cysteine oxidoreductase, dsbD, is identified by genetic selection. The dsbD gene is shown to be essential for cell growth at elevated temperatures (>42°C). A 138 amino acid subdomain of the dsbD gene product exhibits extensive identity with the eukaryotic PDI active-site region and is shown to have oxidoreductase activity in vitro. In addition, in dsbD mutants, the active-site dithiol of DsbC is largely in an oxidized state, suggesting that DsbD acts as a periplasmic reducing source.
-
(1995)
EMBO J
, vol.14
, pp. 3415-3424
-
-
Missiakas, D.1
Schwager, F.2
Raina, S.3
-
25
-
-
0027994090
-
The folding of bovine pancreatic trypsin inhibitor in the Escherichia coli periplasm
-
Ostermeier M, Georgiou G: The folding of bovine pancreatic trypsin inhibitor in the Escherichia coli periplasm. J Biol Chem 1994, 269:21072-21077. The kinetics of folding of BPTI in the periplasmic space of E. coli are determined. Folding in the periplasm is shown to be substantially faster than that in vitro and is absolutely dependent on the prokaryotic enzyme DsbA. Evidence is presented that the rate-limiting step in the folding of this heterologous protein in the periplasmic space is the isomerization of disulfide bonds.
-
(1994)
J Biol Chem
, vol.269
, pp. 21072-21077
-
-
Ostermeier, M.1
Georgiou, G.2
-
26
-
-
0028850389
-
Human protein disulfide isomerase functionally complements a dsbA mutation and enhances the yield of pectate lyase C in Escherichia coli
-
Humphreys DP, Weir N, Mountain A, Lund PA: Human protein disulfide isomerase functionally complements a dsbA mutation and enhances the yield of pectate lyase C in Escherichia coli. J Biol Chem 1995, 270:28210-28215. Human PDI is expressed in the periplasmic space of E. coli and is shown to complement phenotypes associated with DsbA mutations. Expression of human PDI in wild-type cells results in improved yields of active pectate lyase. Similarly, pectin lyase can be produced in DsbA- mutants expressing human PDI when the growth medium is supplemented with oxidized glutathione.
-
(1995)
J Biol Chem
, vol.270
, pp. 28210-28215
-
-
Humphreys, D.P.1
Weir, N.2
Mountain, A.3
Lund, P.A.4
-
27
-
-
0026327753
-
A novel strategy for the production of a highly expressed recombinant protein in an active form
-
Blackwell JR, Horgan R: A novel strategy for the production of a highly expressed recombinant protein in an active form. FEBS Lett 1991, 295:10-12.
-
(1991)
FEBS Lett
, vol.295
, pp. 10-12
-
-
Blackwell, J.R.1
Horgan, R.2
-
28
-
-
0028303849
-
Improved synthesis of Salmonella typhimurium enterotoxin using gene fusion expression systems
-
Chopra AK, Brasier AR, Das M, Xu XJ, Peterson JW: Improved synthesis of Salmonella typhimurium enterotoxin using gene fusion expression systems. Gene 1994, 144:81-85. A fusion of thioredoxin and Salmonella typhimurium enterotoxin is shown to result in enhanced enterotoxin solubility compared with a glutathione fusion or the native enterotoxin. A further increase in expression is obtained by growing the cell in the presence of NaCl.
-
(1994)
Gene
, vol.144
, pp. 81-85
-
-
Chopra, A.K.1
Brasier, A.R.2
Das, M.3
Xu, X.J.4
Peterson, J.W.5
-
29
-
-
0027584038
-
Overcoming inclusion body formation in a high level expression system
-
Moore JT, Arvinder U, Maley F, Maley GF: Overcoming inclusion body formation in a high level expression system Protein Expr Purif 1993, 4:160-163.
-
(1993)
Protein Expr Purif
, vol.4
, pp. 160-163
-
-
Moore, J.T.1
Arvinder, U.2
Maley, F.3
Maley, G.F.4
-
30
-
-
14744292185
-
A thioredoxin gene fusion expression system that circumvents inclusion body formation in the E. coli cytoplasm
-
LaVallie ER, Diblasio EA, Kovacic S, Grant KL, Schendel PF, McCoy JM: A thioredoxin gene fusion expression system that circumvents inclusion body formation in the E. coli cytoplasm. Biotechnology 1993, 11:187-193.
-
(1993)
Biotechnology
, vol.11
, pp. 187-193
-
-
LaVallie, E.R.1
Diblasio, E.A.2
Kovacic, S.3
Grant, K.L.4
Schendel, P.F.5
McCoy, J.M.6
-
31
-
-
0029294021
-
Purification by immobilized metal affinity chromatography of human atrial natriuretic peptide expressed in a novel thioredoxin fusion protein
-
6 metal affinity binding site, followed by E. coli thioredoxin, a factor Xa protease recognition site and ANP.
-
(1995)
Biotechnol Prag
, vol.11
, pp. 265-269
-
-
Wilkinson, D.L.1
Ma, N.T.2
Haught, C.3
Harrison, R.G.4
-
32
-
-
0028314030
-
Enhanced in vitro refolding of insulin-like growth factor I using a solubilizing fusion partner
-
Samuelsson E, Moks T, Nilsson B, Uhlen M: Enhanced in vitro refolding of insulin-like growth factor I using a solubilizing fusion partner. Biochemistry 1994, 33:4207-4211. The refolding in vitro of insulin-like growth factor (IGF)-I, either by itself or fused to one or two Z domains, is investigated. Fusion of IGF-I to one or two Z domains results in a dramatic enhancement of solubility (>100-fold). In addition, fusion to Z domains inhibits IGF-I association during protein renaturation.
-
(1994)
Biochemistry
, vol.33
, pp. 4207-4211
-
-
Samuelsson, E.1
Moks, T.2
Nilsson, B.3
Uhlen, M.4
-
35
-
-
0027157482
-
GroE mediated folding of bacterial luciferases in vivo
-
Escher A, Szalay AA: GroE mediated folding of bacterial luciferases in vivo. Mol Gen Genet 1993, 238:65-73.
-
(1993)
Mol Gen Genet
, vol.238
, pp. 65-73
-
-
Escher, A.1
Szalay, A.A.2
-
36
-
-
0029086245
-
Expression and characterization of branched-chain α-ketoacid dehydrogenase kinase from the rat. Is it a histidine protein kinase?
-
Davie JR, Wynn RM, Meng M, Huang Y-S, Aalund G, Chuang DT, Lau KS: Expression and characterization of branched-chain α-ketoacid dehydrogenase kinase from the rat. Is it a histidine protein kinase? J Biol Chem 1995, 270:19861-19867. Rat branched-chain α-ketoacid dehydrogenase kinase is expressed in E. coli as a fusion protein with bacterial maltose-binding protein. Co-overexpression of the molecular chaperones GroES and GroEL results in a significant increase in the amount of fusion protein expressed in the soluble fraction (a threefold to fourfold yield enhancement). The protein is then purified and its enzymatic activity characterized.
-
(1995)
J Biol Chem
, vol.270
, pp. 19861-19867
-
-
Davie, J.R.1
Wynn, R.M.2
Meng, M.3
Huang, Y.-S.4
Aalund, G.5
Chuang, D.T.6
Lau, K.S.7
-
37
-
-
0026652374
-
2) of mammalian mitochondrial branched-chain α-ketoacid decarboxylase in Escherichia coli
-
2) of mammalian mitochondrial branched-chain α-ketoacid decarboxylase in Escherichia coli. J Biol Chem 1992, 267:12400-12403.
-
(1992)
J Biol Chem
, vol.267
, pp. 12400-12403
-
-
Wynn, R.M.1
Davie, J.R.2
Cox, R.P.3
Chuang, D.T.4
-
38
-
-
0026483711
-
Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli
-
Gragerov A, Nudler E, Komissarova N, Gaitanaris GA, Gottesman ME, Nikiforov V: Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli. Proc Natl Acad Sci USA 1992, 89:10341-10344.
-
(1992)
Proc Natl Acad Sci USA
, vol.89
, pp. 10341-10344
-
-
Gragerov, A.1
Nudler, E.2
Komissarova, N.3
Gaitanaris, G.A.4
Gottesman, M.E.5
Nikiforov, V.6
-
39
-
-
0040424324
-
Overproduction of bacterial chaperones improves the solubility of recombinant protein tyrosine kinases in Escherichia coli
-
Caspers P, Stieger M, Burn P: Overproduction of bacterial chaperones improves the solubility of recombinant protein tyrosine kinases in Escherichia coli. Cell Mol Biol 1994, 40:635-644. Overproduction of molecular chaperones of the GroES/EL and DnaK/J systems is shown to increase the solubility of Csk, Fyn and Lck expressed in E. coli.
-
(1994)
Cell Mol Biol
, vol.40
, pp. 635-644
-
-
Caspers, P.1
Stieger, M.2
Burn, P.3
-
40
-
-
0027436420
-
In vivo control of redox potential during protein folding catalyzed by bacterial protein disulfide isomerase (DsbA)
-
Wunderlich M, Glockshuber R: In vivo control of redox potential during protein folding catalyzed by bacterial protein disulfide isomerase (DsbA). J Biol Chem 1993, 268:24547-24550.
-
(1993)
J Biol Chem
, vol.268
, pp. 24547-24550
-
-
Wunderlich, M.1
Glockshuber, R.2
|