Escherichia coli reconstitution

Tang, M., Bruck, I., Eri a, R., Turner, J., Frank, E. G., Woodgate, R., O Donnell, M., and Goodman, M. F. (1998). Biochemical basis of SOS-induced mutagenesis in Escherichia coli Reconstitution of in vitro lesion bypass dependent on the UmuD 2C mutagenic complex and RecA protein. Proc. Natl. Acad. Sci. USA 95, 9755-9760. 

Ratnatilleke A, JW Vrijbloed, JA Robinson (1999) Cloning and sequencing of the coenzyme B,2-binding domain of isobutyryl-CoA mutase from Streptomyces cinnamonensis. Reconstitution of mutase activity and characterization of the recombinant enzyme produced in Escherichia coli. J Biol Chem 274 31679-31685. 

GILLAM, E.M.J., BABA, T, KIM, B-R., OHMORI, S., GUENGERICH, F.P., Expression of modified human cytochrome P450 3A4 in Escherichia coli and purification and reconstitution of the enzyme, Arch. Biochem. Biophys., 1993, 305, 123-131. 

Vandenbroeck, K., E. Martens, S. D Andrea, and A. Billiau (1993). Refolding and single-step purification of porcine interferon-gamma from Escherichia coli inclusion bodies. Conditions for reconstitution of dimeric IFN-gamma. Eur J Biochem 215(2) 481-486. 

Field, H., G.T. Yarranton, and A.R. Rees, Expression of mouse immunoglobulin light and heavy chain variable regions in Escherichia coli and reconstitution of antigen-binding activity. Protein Eng, 1990. 3(7) 641-7. 

The Mg2+-activated ATPase (or ATP synthase) is made up of two parts. The Fj component is the catalytic, Mg2+-binding, extrinsic membrane protein composed of five different subunits, a, (3, y, S and e. The F0 component is an intrinsic membrane complex that contains three subunits, a, b and c, and mediates proton translocation. The F, protein is bound to the membrane through interaction with F0. The complexity of the F,F0 enzyme has presented many difficulties. Hie greatest advances have been made for the bacterial enzymes, notably for thermophiles, Escherichia coli and Rhodospirillum rubrum, where progress has been made in the purification of subunits and their reconstitution into membranes, and the identification of binding sites for Mg2+ and nucleotides on the Fi subunits.300 FiF0 preparations can be incorporated into liposomes and display H+ translocation, ATP-P, exchange and ATP synthesis.301... 

Schneider, E., and Altendorf, K. (1985). All three subunits are required for the reconstitution of an active proton channel (F0) of Escherichia coli ATP synthase (FjFo). EMBO J. 4, 515-518. 

Newman, M.J. Wilson, T.H. (1980). Solubilization and reconstitution of the lactose transport system from Escherichia coli. J. Biol. Chem. 255,10583-10586. 

Roepe, P.D. Kaback, H.R. (1989). Characterization and functional reconstitution of a soluble form of the hydrophobic membrane protein lac permease from Escherichia coli. Proc. Natl. Acad. Sri. USA 86,6087-6091. 

Although remarkable progress has been made in matching the secondary structure and the function in the various members of the mitochondrial carrier family (del Arco and Satrustegui 2005), satisfying information about the function of potential ADP/ATP transporters can only come from a detailed functional analysis (see later). Several methods are currently available reconstitution in liposomes, in vivo expression, rescue experiments, and functional tests in bacteria (Escherichia coli, Lactococcus lactis). Such tests involve competition experiments, effector and inhibitor studies (Voncken 2001 Voncken et al. 2002a Haferkamp et al. 2002 van der Giezen et al. 2002 Tjaden et al. 2004 Chan et al. 2005 Leroch 2006). 

The Streptomyces lividans K+ channel (KcsA) is a 160-residue protein that forms homotetrameric channels closely related to the pore domain of larger voltage-dependent channels (Schrempf et al., 1995). When purified and reconstituted in lipid bilayers, KcsA catalyzes single-channel activities with selectivity properties identical to those of other eukaryotic K+ channels (Cuello et al., 1998 Heginbotham et al., 1999 Meuser et al., 1999). The fact that KcsA is easily expressed in Escherichia coli at milligram levels made this protein an ideal target for structural analysis. 

Borgnia, M. J., and Agre, P (2001). Reconstitution and functional comparison of purified GlpF and AqpZ, the glycerol and water channels from Escherichia coli. Proc. Natl. Acad. Sci. USA 98, 2888-2893. 

Zylicz, M., Ang, D., Liberek, K., Yamamoto, T., and Georgopoulos, C. (1988). Initiation of lambda DNA replication reconstituted with purified lambda and Escherichia coli replication proteins. Biochim. Biophys. Acta 951, 344-350. 

Tikhonova, E.B., Devroy, V.K., lan S.Y., and Zgurskaya, H.I. (2007) Reconstitution of the Escherichia coli macrolide transporter the periplasmic membrane fusion protein MacA stimulates the ATPase activity of MacB. Molecular Microbiology, 63 (3), 895-910. 

K.A. Mooijman, N.G.W.M. van Strijp-Lockefeer. A.H. Havelaar, R. van der Heide, D. Branger and E.A. Maier, Certification of number concentration of colony forming particles of Escherichia coli in one ml suspension of reconstituted artificially contaminated milk powder CRM 594. Report EUR 16887 EN, CEC Luxembourg (1996). 

Paulsen H, Riimler U and Rudiger W (1990) Reconstitution of pigment-containing complexes from light-harvesting chlorophyll a/b-binding protein overexpressed in Escherichia coli. Planta 181 204-211... 

Nitta, I., Kamada, Y, Noda, H., Ueda, X, and Watanabe, K. (1998). Reconstitution of peptide bond formation with Escherichia coli 23S rRNA ribosomal RNA domains. Science 281, 666-669. 

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