Mutations that alter the equilibrium between open and closed conformations of Escherichia coli maltose-binding protein impede its ability to enhance the solubility of passenger proteins

Biochemical and Biophysical Research Communications

Volumn 364, Issue 3, 2007, Pages 639-644

  Nallamsetty, Sreedevi ^a   Waugh, David S ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

Author keywords

Affinity tag; Fusion protein; Maltose binding protein; Solubility enhancer; Solubility tag

Indexed keywords

HYBRID PROTEIN; MALTOSE BINDING PROTEIN; RECOMBINANT PROTEIN;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; ESCHERICHIA COLI; GENE MUTATION; LIGAND BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FUNCTION; SOLUBILITY;

ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; KINETICS; MUTAGENESIS, SITE-DIRECTED; PERIPLASMIC BINDING PROTEINS; PROTEIN CONFORMATION; PROTEIN TRANSPORT; RECOMBINANT PROTEINS; SOLUBILITY; STRUCTURE-ACTIVITY RELATIONSHIP;

ESCHERICHIA COLI;

EID: 35648941605     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.10.060     Document Type: Article

References (24)

1. Waugh D.S. Making the most of affinity tags. Trends Biotechnol. 23 (2005) 316-320
2. Esposito D., and Chatterjee D.K. Enhancement of soluble protein expression through the use of fusion tags. Curr. Opin. Biotechnol. 17 (2006) 353-358
3. Kapust R.B., and Waugh D.S. Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused. Protein Sci. 8 (1999) 1668-1674
4. Hammarström M., Hellgren N., Van den Berg S., Berglund H., and Härd T. Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli. Protein Sci. 11 (2002) 313-321
5. Shih Y.P., Kung W.M., Chen J.C., Yeh C.H., Wang A.H.J., and Wang T.F. High-throughput screening of soluble recombinant proteins. Protein Sci. 11 (2002) 1714-1719
6. M.R. Dyson, S.P. Shadbolt, K.J. Vincent, R.L. Perera, J. McCafferty, Production of soluble mammalian proteins in Escherichia coli: identification of protein features that correlate with successful expression, BMC Biotechnol. 4 (32) (2004), doi: 10.1186/1472-6750-4-32.
7. Pryor K.D., and Leiting B. High-level expression of soluble protein in Escherichia coli using a His6-tag and maltose-binding protein double-affinity fusion system. Protein Expr. Purif. 10 (1997) 309-319
8. Routzahn K.M., and Waugh D.S. Differential effects of supplementary affinity tags on the solubility of MBP fusion proteins. J. Struct. Funct. Genomics 2 (2002) 83-92
9. Telmer P.G., and Shilton B.H. Insights into the conformational equilibria of maltose-binding protein by analysis of high affinity mutants. J. Biol. Chem. 278 (2003) 34555-34567
10. Marvin J.S., and Hellinga H.W. Manipulation of ligand binding affinity by exploitation of conformational coupling. Nat. Struct. Biol. 8 (2001) 795-798
11. Fox J.D., and Waugh D.S. Maltose-binding protein as a solubility enhancer. Methods Mol. Biol. 205 (2003) 99-117
12. Nallamsetty S., Austin B.P., Penrose K.J., and Waugh D.S. Gateway vectors for the production of combinatorially-tagged His6-MBP fusion proteins in the cytoplasm and periplasm of Escherichia coli. Protein Sci. 14 (2005) 2964-2971
13. Nallamsetty S., and Waugh D.S. Solubility-enhancing proteins MBP and NusA play a passive role in the folding of their fusion partners. Protein Expr. Purif. 45 (2006) 175-182
14. Nallamsetty S., Kapust R.B., Tozser J., Cherry S., Tropea J.E., Copeland T.D., and Waugh D.S. Efficient site-specific processing of fusion proteins by tobacco vein mottling virus protease in vivo and in vitro. Protein Expr. Purif. 38 (2004) 108-115
15. Shirley B.A. Urea and guanidine hydrochloride denaturation curves. Methods Mol. Biol. 40 (1995) 177-190
16. Nallamsetty S., Dubey V.K., Pande M., Ambasht P.K., and Jagannadham M.V. Accumulation of partly folded states in the equilibrium unfolding of ervatamin A: spectroscopic description of the native, intermediate, and unfolded states. Biochimie 89 (2007) 1416-1424
17. Sharff A.J., Rodseth L.E., Spurlino J.C., and Quiocho F.A. Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis. Biochemistry 31 (1992) 10657-10663
18. Fox J.D., Routzahn K.M., Bucher M.H., and Waugh D.S. Maltodextrin-binding proteins from diverse bacteria and archaea are potent solubility enhancers. FEBS Lett. 537 (2003) 53-57
19. Fox J.D., Kapust R.B., and Waugh D.S. Single amino acid substitutions on the surface of Escherichia coli maltose-binding protein can have a profound impact on the solubility of fusion proteins. Protein Sci. 10 (2001) 622-630
20. Nomine Y., Ristriani T., Laurent C., Lefevre J.F., Weiss E., and Trave G. Formation of soluble inclusion bodies by HPV E6 oncoprotein fused to maltose-binding protein. Protein Expr. Purif. 23 (2001) 22-32
21. Douette P., Navet R., Gerkens P., Galleni M., Lévy D., and Sluse F.E. Escherichia coli fusion carrier proteins act as solubilizing agents for recombinant uncoupling protein 1 through interactions with GroEL. Biochem. Biophys. Res. Commun. 333 (2005) 686-693
22. Huang Y.S., and Chuang D.T. Mechanisms for GroEL/GroES-mediated folding of a large 86-kDa fusion polypeptide in vitro. J. Biol. Chem. 274 (1999) 10405-10412
23. Zhang Y.B., Howitt J., McCorkle S., Lawrence P., Springer K., and Freimuth P. Protein aggregation during overexpression limited by peptide extensions with large net negative charge. Protein Expr. Purif. 36 (2004) 207-216
24. Su Y., Zou Z., Feng S., Zhou P., and Cao L. The acidity of protein fusion partners predominantly determines the efficacy to improve the solubility of the target proteins expressed in Escherichia coli. J. Biotech. 129 (2007) 373-382