Production in Escherichia coli of a recombinant C-terminal truncated precursor of surfactant protein B (rproSP-BΔc). Structure and interaction with lipid interfaces

Biochimica et Biophysica Acta - Biomembranes

Volumn 1758, Issue 10, 2006, Pages 1621-1632

  Serrano, Alicia G ^a   Cabré, Elisa J ^a   Oviedo, José M ^a   Cruz, Antonio ^a   González, Beatriz ^a   Palacios, Alicia ^a   Estrada, Pilar ^a   Pérez Gil, Jesús ^a  

^a UNIVERSIDAD COMPLUTENSE DE MADRID   (Spain)

Author keywords

Amphipathic protein; Inclusion body; Lipid protein interaction; Lung surfactant; Protein folding; Saposin like protein

Indexed keywords

LUNG SURFACTANT; MEMBRANE PROTEIN; PHOSPHOLIPID; RECOMBINANT PROTEIN; SURFACTANT PROTEIN B; TRYPTOPHAN;

ADSORPTION; AMINO TERMINAL SEQUENCE; ARTICLE; BACTERIUM CULTURE; CARBOXY TERMINAL SEQUENCE; CELL INCLUSION; CIRCULAR DICHROISM; ELECTROPHORETIC MOBILITY; ESCHERICHIA COLI; FLUORESCENCE SPECTROSCOPY; GENE OVEREXPRESSION; HYDROPHOBICITY; IMMUNOREACTIVITY; LIPID BILAYER; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN LIPID INTERACTION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; BLOTTING, WESTERN; CIRCULAR DICHROISM; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ESCHERICHIA COLI; HUMANS; MOLECULAR SEQUENCE DATA; PROTEIN FOLDING; PROTEIN PRECURSORS; PROTEOLIPIDS; RECOMBINANT PROTEINS; SPECTROPHOTOMETRY, ULTRAVIOLET;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 33749049579     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2006.07.016     Document Type: Article

References (41)

1. Melton K.R., Nesslein L.L., Ikegami M., Tichelaar J.W., Clark J.C., Whitsett J.A., and Weaver T.E. SP-B deficiency causes respiratory failure in adult mice. Am. J. Physiol.: Lung Cell Mol. Physiol. 285 (2003) L543-L549
2. Nesslein L.L., Melton K.R., Ikegami M., Na C.L., Wert S.E., Rice W.R., Whitsett J.A., and Weaver T.E. Partial SP-B deficiency perturbs lung function and causes air space abnormalities. Am. J. Physiol.: Lung Cell Mol. Physiol. 288 (2005) L1154-L1161
3. Nogee L.M., Garnier G., Dietz H.C., Singer L., Murphy A.M., deMello D.E., and Colten H.R. A mutation in the surfactant protein B gene responsible for fatal neonatal respiratory disease in multiple kindreds. J. Clin. Invest. 93 (1994) 1860-1863
4. Nogee L.M., Wert S.E., Proffit S.A., Hull W.M., and Whitsett J.A. Allelic heterogeneity in hereditary surfactant protein B (SP-B) deficiency. Am. J. Respir. Crit. Care Med. 161 (2000) 973-981
5. Korimilli A., Gonzales L.W., and Guttentag S.H. Intracellular localization of processing events in human surfactant protein B biosynthesis. J. Biol. Chem. 275 (2000) 8672-8679
6. Ueno T., Linder S., Na C.L., Rice W.R., Johansson J., and Weaver T.E. Processing of pulmonary surfactant protein B by napsin and cathepsin H. J. Biol. Chem. 279 (2004) 16178-16184
7. Oosterlaken-Dijksterhuis M.A., van Eijk M., van Golde L.M., and Haagsman H.P. Lipid mixing is mediated by the hydrophobic surfactant protein SP-B but not by SP-C. Biochim. Biophys. Acta 1110 (1992) 45-50
8. Poulain F.R., Allen L., Williams M.C., Hamilton R.L., and Hawgood S. Effects of surfactant apolipoproteins on liposome structure: implications for tubular myelin formation. Am. J. Physiol. 262 (1992) L730-L739
9. Poulain F.R., Nir S., and Hawgood S. Kinetics of phospholipid membrane fusion induced by surfactant apoproteins A and B. Biochim. Biophys. Acta 1278 (1996) 169-175
10. Ryan M.A., Qi X., Serrano A.G., Ikegami M., Perez-Gil J., Johansson J., and Weaver T.E. Mapping and analysis of the lytic and fusogenic domains of surfactant protein B. Biochemistry 44 (2005) 861-872
11. Lin S., Phillips K.S., Wilder M.R., and Weaver T.E. Structural requirements for intracellular transport of pulmonary surfactant protein B (SP-B). Biochim. Biophys. Acta 1312 (1996) 177-185
12. Lin S., Akinbi H.T., Breslin J.S., and Weaver T.E. Structural requirements for targeting of surfactant protein B (SP-B) to secretory granules in vitro and in vivo. J. Biol. Chem. 271 (1996) 19689-19695
13. Akinbi H.T., Breslin J.S., Ikegami M., Iwamoto H.S., Clark J.C., Whitsett J.A., Jobe A.H., and Weaver T.E. Rescue of SP-B knockout mice with a truncated SP-B proprotein. Function of the C-terminal propeptide. J. Biol. Chem. 272 (1997) 9640-9647
14. Polayes D., and Hughes J. Efficient protein expression and simple purification using the pProEx-1 system. Focus 16 (1994) 81-84
15. Sechi S., and Chait B.T. Modification of cysteine residues by alkylation. A tool in peptide mapping and protein identification. Anal. Chem. 70 (1998) 5150-5158
16. Ellman G.L. A colorimetric method for determining low concentrations of mercaptans. Arch. Biochem. Biophys. 74 (1958) 443-450
17. Ellman G.L. Tissue sulfhydryl groups. Arch. Biochem. Biophys. 82 (1959) 70-77
18. Ruano M.L., Garcia-Verdugo I., Miguel E., Perez-Gil J., and Casals C. Self-aggregation of surfactant protein A. Biochemistry 39 (2000) 6529-6537
19. Sreerama N., and Woody R.W. Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem. 287 (2000) 252-260
20. Sreerama N., and Woody R.W. On the analysis of membrane protein circular dichroism spectra. Protein Sci. 13 (2004) 100-112
21. Nuñez E., Wei X., Delgado C., Rodriguez-Crespo I., Yelamos B., Gomez-Gutierrez J., Peterson D.L., and Gavilanes F. Cloning, expression, and purification of histidine-tagged preS domains of hepatitis B virus. Protein Expr. Purif. 21 (2001) 183-191
22. Serrano A.G., Cruz A., Rodriguez-Capote K., Possmayer F., and Perez-Gil J. Intrinsic structural and functional determinants within the amino acid sequence of mature pulmonary surfactant protein SP-B. Biochemistry 44 (2005) 417-430
23. Lakowicz J.R. Principles of Fluorescence Spectroscopy (1999), Plenum Press, New York
24. Brockman H. Lipid monolayers: why use half a membrane to characterize protein-membrane interactions?. Curr. Opin. Struct. Biol. 9 (1999) 438-443
25. Zaltash S., and Johansson J. Secondary structure and limited proteolysis give experimental evidence that the precursor of pulmonary surfactant protein B contains three saposin-like domains. FEBS Lett. 423 (1998) 1-4
26. H.T. Akinbi, P. Markart, R. Epaud, Z.C. Chroneos, T.E. Weaver, Antibacterial properties of surfactant protein B in innate host defense of the lung, (2005).
27. Hawgood S. Surfactant protein B: structure and function. Biol. Neonate 85 (2004) 285-289
28. Brasch F., Ochs M., Kahne T., Guttentag S., Schauer-Vukasinovic V., Derrick M., Johnen G., Kapp N., Muller K.M., Richter J., Giller T., Hawgood S., and Buhling F. Involvement of napsin A in the C- and N-terminal processing of surfactant protein B in type-II pneumocytes of the human lung. J. Biol. Chem. 278 (2003) 49006-49014
29. Brasch F., Johnen G., Winn-Brasch A., Guttentag S.H., Schmiedl A., Kapp N., Suzuki Y., Muller K.M., Richter J., Hawgood S., and Ochs M. Surfactant protein B in type II pneumocytes and intra-alveolar surfactant forms of human lungs. Am. J. Respir. Cell Mol. Biol. 30 (2004) 449-558
30. Qi X., Leonova T., and Grabowski G.A. Functional human saposins expressed in Escherichia coli. Evidence for binding and activation properties of saposins C with acid beta-glucosidase. J. Biol. Chem. 269 (1994) 16746-16753
31. Holzinger A., Phillips K.S., and Weaver T.E. Single-step purification/solubilization of recombinant proteins: application to surfactant protein B. BioTechniques 20 (1996) 804-806 (808)
32. Andersson M., Curstedt T., Jornvall H., and Johansson J. An amphipathic helical motif common to tumourolytic polypeptide NK-lysin and pulmonary surfactant polypeptide SP-B. FEBS Lett. 362 (1995) 328-332
33. O'Brien J.S., and Kishimoto Y. Saposin proteins: structure, function, and role in human lysosomal storage disorders. FASEB J. 5 (1991) 301-308
34. Perez-Gil J., Cruz A., and Casals C. Solubility of hydrophobic surfactant proteins in organic solvent/water mixtures. Structural studies on SP-B and SP-C in aqueous organic solvents and lipids. Biochim. Biophys. Acta 1168 (1993) 261-270
35. Waring A.J., Chen Y., Faull K.F., Stevens R., Sherman M.A., and Fluharty A.L. Porcine cerebroside sulfate activator (saposin B) secondary structure: CD, FTIR, and NMR studies. Mol. Genet. Metab. 63 (1998) 14-25
36. Hawgood S., Latham D., Borchelt J., Damm D., White T., Benson B., and Wright J.R. Cell-specific posttranslational processing of the surfactant-associated protein SP-B. Am. J. Physiol. 264 (1993) L290-L299
37. O'Reilly M.A., Weaver T.E., Pilot-Matias T.J., Sarin V.K., Gazdar A.F., and Whitsett J.A. In vitro translation, post-translational processing and secretion of pulmonary surfactant protein B precursors. Biochim. Biophys. Acta 1011 (1989) 140-148
38. Kaderbhai M.A., and Austen B.M. Studies on the formation of intrachain disulphide bonds in newly biosynthesised bovine prolactin. Role of protein-disulphide isomerase. Eur. J. Biochem. 153 (1985) 167-178
39. Lee H., Kim H.K., Lee J.H., You W.K., Chung S.I., Chang S.I., Park M.H., Hong Y.K., and Joe Y.A. Disruption of interkringle disulfide bond of plasminogen kringle 1-3 changes the lysine binding capability of kringle 2, but not its antiangiogenic activity. Arch. Biochem. Biophys. 375 (2000) 359-363
40. Cruz A., Worthman L.A., Serrano A.G., Casals C., Keough K.M., and Perez-Gil J. Microstructure and dynamic surface properties of surfactant protein SP-B/dipalmitoylphosphatidylcholine interfacial films spread from lipid-protein bilayers. Eur. Biophys. J. 29 (2000) 204-213
41. Beers M.F. Inhibition of cellular processing of surfactant protein C by drugs affecting intracellular pH gradients. J. Biol. Chem. 271 (1996) 14361-14370