Effect of Signal Peptide on the Stability and Folding Kinetics of Maltose Binding Protein

Biochemistry

Volumn 43, Issue 12, 2004, Pages 3608-3619

  Beena, K ^a   Udgaonkar, Jayant B ^b   Varadarajan, R ^a  

^a INDIAN INSTITUTE OF SCIENCE   (India)

^b TATA INSTITUTE OF FUNDAMENTAL RESEARCH   (India)

Author keywords

[No Author keywords available]

Indexed keywords

CHARACTERIZATION; HYDROPHOBICITY; REACTION KINETICS; THERMODYNAMICS;

FOLDING KINETICS; THERMAL DENATURATION;

PROTEINS;

MALTOSE BINDING PROTEIN; PROTEIN PRECURSOR; PROTEINASE; SIGNAL PEPTIDE; UREA;

ARTICLE; BINDING KINETICS; CELL COMPARTMENTALIZATION; CELL SPECIFICITY; CELLULAR DISTRIBUTION; DENATURATION; ESCHERICHIA COLI; GENE TRANSLOCATION; HYDROPHOBICITY; ISOTHERM; NONHUMAN; PEPTIDE ANALYSIS; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STABILITY; PROTEIN TARGETING; SEQUENCE ANALYSIS; THERMODYNAMICS;

BACTERIAL PROTEINS; CARRIER PROTEINS; CIRCULAR DICHROISM; ESCHERICHIA COLI PROTEINS; GUANIDINE; HYDROLYSIS; KINETICS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN PRECURSORS; PROTEIN RENATURATION; PROTEIN SORTING SIGNALS; SPECTROMETRY, FLUORESCENCE; SUBSTRATE SPECIFICITY; TEMPERATURE; THERMODYNAMICS; UREA;

ESCHERICHIA COLI; NEGIBACTERIA;

EID: 1642348275     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0360509     Document Type: Article

References (40)

1. Blobel, G., and Dobberstein, B. (1975) Transfer of proteins across membranes. I. Presence of proteolytically processed and unprocessed nascent immunoglobulin light chains on membrane-bound ribosomes of murine myeloma. J. Cell Biol. 67, 835-851.
2. Milstein, C., Brownlee, G. G., Harrison, T. M., and Mathews, M. B. (1972) A possible precursor of immunoglobulin light chains. Nat. New Biol. 239, 117-120.
3. von Heijne, G., and Blomberg, C. (1979) Trans-membrane translocation of proteins. The direct transfer model. Eur. J. Biochem. 97, 175-181.
4. Engelman, D. M., and Steitz, T. A. (1981) The spontaneous insertion of proteins into and across membranes: the helical hairpin hypothesis. Cell 23, 411-422.
5. Inouye, M., and Halegoua, S. (1980) Secretion and membrane localization of proteins in Escherichia coli. CRC Crit. Rev. Biochem. 7, 339-371.
6. Park, S., Liu, G., Topping, T. B., Cover, W. H., and Randall, L. L. (1988) Modulation of folding pathways of exported proteins by the leader sequence. Science 239, 1033-1035.
7. Lee, H., Chi, S. W., Kang, M., Baek, K., and Kim, H. (1996) Stability and folding of precursor and mature tryptophan-substituted ribose binding protein of Escherichia coli. Arch. Biochem. Biophys. 328, 78-84.
8. Goder, V., Beckert, V., Pfeil, W., and Bernhardt, R. (1998) Impact of the presequence of a mitochondrium-targeted precursor, preadrenodoxin, on folding, catalytic activity, and stability of the protein in vitro. Arch Biochem. Biophys. 359, 31-41.
9. Liu, G. P., Topping, T. B., Cover, W. H., and Randall, L. L. (1988) Retardation of folding as a possible means of suppression of a mutation in the leader sequence of an exported protein. J. Biol. Chem. 263, 14790-14793.
10. Diamond, D. L., Strobel, S., Chun, S. Y., and Randall, L. L. (1995) Interaction of SecB with intermediates along the folding pathway of maltose-binding protein. Protein Sci. 4, 1118-1123.
11. Raffy, S., Sassoon, N., Hofnung, M., and Betton, J. M. (1998) Tertiary structure-dependence of misfolding substitutions in loops of the maltose-binding protein. Protein Sci. 7, 2136-2142.
12. Chun, S. Y., Strobel, S., Bassford, P., Jr., and Randall, L. L. (1993) Folding of maltose-binding protein. Evidence for the identity of the rate-determining step in vivo and in vitro. J. Biol. Chem. 268, 20855-20862.
13. Hardy, S. J., and Randall, L. L. (1991) A kinetic partitioning model of selective binding of nonnative proteins by the bacterial chaperone SecB. Science 251, 439-443.
14. Collier, D. N. (1993) SecB: a molecular chaperone of Escherichia coli protein secretion pathway. Adv. Protein Chem. 44, 151-193.
15. Lecker, S. H., Driessen, A. J., and Wickner, W. (1990) ProOmpA contains secondary and tertiary structure prior to translocation and is shielded from aggregation by association with SecB protein. EMBO J. 9, 2309-2314.
16. Fekkes, P., den Blaauwen, T., and Driessen, A. J. (1995) Diffusion-limited interaction between unfolded polypeptides and the Escherichia coli chaperone SecB. Biochemistry 34, 10078-10085.
17. Panse, V. G., Udgaonkar, J. B., and Varadarajan, R. (1998) SecB binds only to a late nativelike intermediate in the folding pathway of barstar and not to the unfolded state. Biochemistry 37, 14477-14483.
18. Prajapati, R. S., Lingaraju, G. M., Bacchawat, K., Surolia, A., and Varadarajan, R. (2003) Thermodynamic effects of replacements of Pro residues in helix interiors of Maltose Binding Protein. Proteins 53, 863-871.
19. Kellermann, O. K., and Ferenci, T. (1982) Maltose-binding protein from Escherichia coli. Methods Enzymol. 90, 459-463.
20. Ferenci, T., and Klotz, U. (1978) Affinity chromatographic isolation of the periplasmic maltose binding protein of Escherichia coli. FEBS Lett 94, 213-217.
21. Szmelcman, S., Schwartz, M., Silhavy, T. J., and Boos, W. (1976) Maltose transport in Escherichia coli K12. A comparison of transport kinetics in wild-type and lambda-resistant mutants as measured by fluorescence quenching. Eur. J. Biochem. 65, 13-9.
22. Ganesh, C., Shah, A. N., Swaminathan, C. P., Surolia, A., and Varadarajan, R. (1997) Thermodynamic characterization of the reversible, two-state unfolding of maltose binding protein, a large two-domain protein. Biochemistry 36, 5020-5028.
23. Pace, C. N. (1986) Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol 131, 266-280.
24. Sheshadri, S., Lingaraju, G. M., and Varadarajan, R. (1999) Denaturant mediated unfolding of both native and molten globule states of maltose binding protein are accompanied by large deltaCp's. Protein Sci. 8, 1689-1695.
25. Agashe, V. R., and Udgaonkar, J. B. (1995) Thermodynamics of denaturation of barstar: evidence for cold denaturation and evaluation of the interaction with guanidine hydrochloride. Biochemistry 34, 3286-3299.
26. Ferenci, T., and Randall, L, L. (1979) Precursor maltose-binding protein is active in binding substrate. J. Biol. Chem. 254, 9979-9981.
27. Randall, L. L., and Hardy, S. J. (1986) Correlation of competence for export with lack of tertiary structure of the mature species: a study in vivo of maltose-binding protein in E. coli. Cell 46, 921-928.
28. Myers, J. K., Pace, C. N., and Scholtz, J. M. (1995) Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding. Protein Sci. 4, 2138-2148.
29. Spurlino, J. C., Lu, G. Y., and Quiocho, F. A. (1991) The 2.3-Å resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis. J. Biol. Chem. 266, 5202-5219.
30. Dierstein, R., and Wickner, W. (1985) The leader region of premaltose binding protein binds amphiphiles. A model for self-assembly in protein export. J. Biol. Chem. 260, 15919-15924.
31. Collier, D. N., Bankaitis, V. A., Weiss, J. B., and Bassford, P. J. J. (1988) The antifolding activity of SecB promotes the export of the E. coli maltose-binding protein. Cell 53, 273-283.
32. Creighton, T. E., and Shortle, D. (1994) Electrophoretic characterization of the denatured states of staphylococcal nuclease. J. Mol. Biol. 242, 670-682.
33. Soulages, J. L. (1998) Chemical denaturation: potential impact of undetected intermediates in the free energy of unfolding and m-values obtained from a two-state assumption. Biophys. J. 75, 484-492.
34. Spudich, G., and Marqusee, S. (2000) A change in the apparent m value reveals a populated intermediate under equilibrium conditions in Escherichia coli ribonuclease HI. Biochemistry 39, 11677-11683.
35. Topping, T. B., and Randall, L. L. (1994) Determination of the binding frame within a physiological ligand for the chaperone SecB. Protein Sci. 3, 730-736.
36. Knoblauch, N. T., Rudiger, S., Schonfeld, H. J., Driessen, A. J., Schneider-Mergener, J., and Bukau, B. (1999) Substrate specificity of the SecB chaperone. J. Biol. Chem. 274, 34219-34225.
37. Liu, G., Topping, T. B., and Randall, L. L. (1989) Physiological role during export for the retardation of folding by the leader peptide of maltose-binding protein. Proc. Natl. Acad. Sci. U.S.A. 86, 9213-9217.
38. Chaudhuri, T. K., Horii, K., Yoda, T., Arai, M., Nagata, S., Terada, T. P., Uchiyama, H., Ikura, T., Tsumoto, K., Kataoka, H., Matsushima, M., Kuwajima, K., and Kumagai, I. (1999) Effect of the extra n-terminal methionine residue on the stability and folding of recombinant alpha-lactalbumin expressed in Escherichia coli. J. Mol. Biol. 285, 1179-1194.
39. Ishikawa, N., Chiba, T., Chen, L. T., Shimizu, A., Ikeguchi, M., and Sugai, S. (1998) Remarkable destabilization of recombinant alpha-lactalbumin by an extraneous N-terminal methionyl residue. Protein Eng. 11, 333-335.
40. Ganesh, C., Banerjee, A., Shah, A., and Varadarajan, R. (1999) Disordered N-terminal residues affect the folding thermodynamics and kinetics of maltose binding protein. FEBS Lett. 454, 307-311.