Enhancing Solubility

From: Subject: Enhancing Solubility Date: Tue, 18 Dec 2007 10:18:05 +0200 MIME-Version: 1.0 Content-Type: multipart/related; type="text/html"; boundary="----=_NextPart_000_0000_01C8415F.4720CE50" X-MimeOLE: Produced By Microsoft MimeOLE V6.00.2900.3198 This is a multi-part message in MIME format. ------=_NextPart_000_0000_01C8415F.4720CE50 Content-Type: text/html; charset="windows-1255" Content-Transfer-Encoding: quoted-printable Content-Location: http://www.emdbiosciences.com/print/NVG/solubility.html?x=9&y=14 Enhancing Solubility

=20

The choice = of vector=20 and expression host can significantly increase the activity = and=20 amount of target protein present in the soluble fraction. A = vector=20 can enhance solubility and/or folding in one of three = ways=96=20
1) provide for fusion to a polypeptide that itself is = highly=20 soluble (e.g. GST, Trx, NusA)
2) provide for fusion to = an enzyme=20 that catalyzes disulfide bond formation (e.g. thioredoxin, = DsbA,=20 DsbC)
3) provide a signal sequence for translocation = into the=20 periplasmic space=20

When using vectors designed for cytoplasmic expression, = folding=20 can be improved in hosts that are permissive for the = formation of=20 disulfide bonds in the cytoplasm. The thioredoxin reductase=20 (trxB) mutation has been shown to allow the formation = of=20 disulfide bonds in the E. coli cytoplasm, which is = further=20 enhanced by the additional mutation in the glutathione = reductase=20 (gor) gene in Origami=99 and Rosetta-gami=99 = hosts.

Fusion Tags in pET Vectors

Cytoplasmic = Localization

The pET-44,=20 pET-43.1 and pET-32 vectors incorporate fusion tags = specifically=20 designed to enhance the solubility of target proteins in the = E.=20 coli cytoplasm. These vectors are also compatible with=20 trxB mutant hosts AD494 and BL21trxB, and with = the=20 trxB/gor mutant Origami, Origami B, and = Rosetta-gami=20 strains.=20

Nus=95Tag=99 sequence: = pET-43.1 and=20 pET-44 series
The pET-43.1 and pET-44 vectors = incorporate the=20 495 aa solubility-promoting NusA (Nus=95Tag) sequence, which = was=20 discovered through a systematic search for E. coli = proteins=20 that have the highest potential for solubility when = overexpressed.=20 [Harrison, R. (2000) inNovations 11,=20 4=967; Novy, R. and Drott, D. (2002) inNovations 14,=20 12-13]

Trx=95Tag=99 sequence: = pET-32=20 series
Many proteins that are normally produced in an = insoluble form in E. coli tend to become more soluble = when=20 fused with the 109 aa N-terminal thioredoxin (Trx=95Tag) = sequence. The=20 Trx=95Tag expressed from pET-32 vectors not only enhances = the=20 solubility of many target proteins, but appears to catalyze = the=20 formation of disulfide bonds in the cytoplasm of trxB = mutants=20 [Stewart et al. (1998) EMBO J. 17, 5543=965550].

GST=95Tag=99 sequence: = pET-41 and 42=20 series
Schistosomal glutathione-S-transferase (GST) = is=20 commonly used as an N-terminal fusion partner when = expressing=20 proteins in E. coli. Although not specifically designed for = this=20 purpose, the 220 aa GST=95Tag sequence has been reported to = enhance=20 the solubility of its fusion partners. The pET-41 and -42 = series of=20 vectors encode the GST=95Tag sequence driven by the powerful = T7lac promoter. Note that these vectors carry = kanamycin=20 resistance, so are not recommended for use with trxB = mutant=20 hosts.=20

Periplasmic = Localization

pET Dsb Fusion Systems 39b and=20 40b
DsbA and DsbC are periplasmic enzymes = that=20 catalyze the formation and isomerization of disulfide bonds, = respectively. The 208 aa DsbA=95Tag=99 [pET-39b(+)] and 236 = aa DsbC=95Tag=99=20 [pET-40b(+)] vectors enable fusion of target polypeptides to = these=20 enzymes, which include their N-terminal secretion signals. = If the=20 fusion protein is exported to the periplasm, the Dsb partner = can=20 assist in proper disulfide bond formation. Note that other = pET=20 vectors that carry signal sequences without the additional = DsbA or=20 DsbC coding regions are also available (pET-12 with ompT = signal=20 sequence; and pET-20, pET-22, pET-25, pET-26, and pET-27 with pelB = signal=20 sequence).=20

Features Common to
Above Vectors

=95	Tightly = controlled=20 T7lac promoter and optimal bacterial ribosome = binding=20 site
=95	Internal 6 aa=20 His=95Tag^=AE (N-terminal in pET-44) and 15 = aa S=95Tag=99=20 sequences for efficient affinity purification and = detection by=20 homogeneous FRET assay, Western blot, and = immunofluorescence=20
=95	Thrombin and=20 Enterokinase cleavage sites for complete N-terminal = tag=20 removal (pET-42 has thrombin and enterokinase or = factor Xa=20 sites)
=95	Multiple cloning=20 sites in all three reading frames [except for = pET-39b(+),=20 40b(+)]
=95	Optional C-terminal=20 HSV=95Tag^=AE epitope and His=95Tag = sequences
=95	Most = available as=20 linearized vectors prepared for efficient, directional = ligation-independent cloning (LIC) of PCR products=20

E. coli Host Strains

Tuner
Tuner=99 = strains are=20 lacYZ deletion mutants of the popular = protease-deficient BL21=20 strain, and enable adjustable levels of protein expression=20 throughout all cells in a culture. The lac permease = (lacY)=20 mutation allows uniform entry of IPTG into all cells in the=20 population, which produces a concentration-dependent, = homogeneous=20 level of induction. By adjusting the concentration of IPTG,=20 expression can be regulated from very low level expression = up to the=20 robust, fully induced expression levels commonly associated = with pET=20 vectors. Lower level expression may enhance the solubility = and=20 activity of difficult target proteins.=20

Rosetta
Rosetta=99 strains=20 are derived from Tuner strains, hence they possess the same=20 advantages afforded by the lacYZ mutation and BL21=20 background. However, Rosetta strains carry an additional = feature,=20 the pRARE plasmid, which encodes tRNAs for mammalian codons = that=20 rarely occur in E. coli, and therefore enhances the=20 expression levels of proteins otherwise limited by codon = usage [Novy=20 et al. (2001) inNovations=20 12, 1=964]. The pRARE plasmid is = selectable on=20 chloramphenicol and is compatible with all pET vectors.=20

Origami
Origami = host=20 strains are K-12 derivatives that have mutations in both the = thioredoxin reductase (trxB) and glutathione = reductase=20 (gor) genes, the combination of which greatly = enhances=20 disulfide bond formation in the cytoplasm [Prinz et al. = (1997) J.=20 Biol. Chem. 272, 15661=9615667]. Studies have shown = that=20 expression in Origami(DE3) yielded 10-fold more active = protein than=20 in a standard host even though overall expression levels = were=20 similar. Origami hosts are compatible with = ampicillin-resistant=20 plasmids and are ideal for use with pET-43.1, pET-44 and = pET-32=20 series vectors.

Origami B
Origami = B host=20 strains combine the protein-folding benefits of Origami = E.=20 coli with precise control of expression levels in Tuner = strains=20 (see above). These strains have the protease-deficient = genetic=20 background of BL21 and are compatible with = ampicillin-resistant=20 plasmids.=20

Rosetta-gami
Rosetta-gami=20 strains are derived from Origami strains, and carry the = pRARE=20 plasmid for rare tRNAs in a K-12 background with the=20 trxB/gor mutations for enhanced disulfide bond = formation in the cytoplasm. These strains are compatible = with=20 ampicillin-resistant vectors, such as the pET-43.1, pET-44 = and=20 pET-32 series.=20

AD494
AD494 = strains are=20 K-12 derived thioredoxin reductase (trxB) mutants = that enable=20 disulfide bond formation in the cytoplasm. The trxB = mutation=20 is selectable on kanamycin; therefore, this strain is = recommended=20 for use with plasmids carrying the ampicillin resistance = marker=20 bla.=20

BL21trxB
BL21trxB=20 strains possess the same thioredoxin reductase mutation=20 (trxB) as the AD494 strains in the protease deficient = BL21=20 background, this strain is recommended for use with plasmids = carrying the ampicillin resistance marker bla.

And for Protein Extraction...
Novagen has developed a family of reagents designed for = simple,=20 efficient extraction of soluble proteins from E. coli = without=20 mechanical disruption. BugBuster=99 Protein Extraction = Reagent=20 is a proprietary mixture of detergents that perforates the = cell wall=20 without denaturing proteins. BugBuster comes as a = ready-to-use=20 reagent for direct resuspension of bacterial pellets, and is = also=20 available as a 10X concentrate to enable = user=20 control of pH, concentration, and buffer additives. The = addition of=20 a small amount of lysozyme along with BugBuster increases = the=20 extraction efficiency and cell lysis, which can increase the = yield=20 of larger target proteins. BugBuster is compatible with Benzonase^=AE = Nuclease, a=20 broad spectrum nuclease that degrades all forms of DNA and = RNA, for=20 efficient viscosity reduction and nucleic acid removal of = protein=20 samples. Protease inhibitors are also available for use with = BugBuster reagents.=20
BugBuster HT combines = BugBuster=20 Protein Extraction Reagent and Benzonase in one convenient = solution,=20 and is well-suited for processing multiple samples. For = automated=20 procedures and other high-throughput applications, Novagen = has=20 developed the novel PopCulture=99 Reagent. This = detergent-based concentrate is added directly to cell = cultures for=20 extraction of proteins without the need for centrifugation = or other=20 cell collection methods [Grabski et al. (2001) inNovations 13,=20 1=964].

=A92007 = Calbiochem,=20 Novabiochem, & Novagen
are brands of EMD Chemicals = Inc., an=20 Affiliate of Merck KGaA, Darmstadt, Germany. =

=0A= _uacct =3D "UA-200617-4";=0A= urchinTracker();=0A=

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