Temperature-induced conformational changes within the regulatory loops L1-L2-LA of the HtrA heat-shock protease from Escherichia coli

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1794, Issue 11, 2009, Pages 1573-1582

  Sobiecka Szkatula, Anna ^a   Polit, Agnieszka ^b   Scire, Andrea ^c   Gieldon, Artur ^a   Tanfani, Fabio ^c   Szkarlat, Zaneta ^a   Ciarkowski, Jerzy ^a   Zurawa Janicka, Dorota ^a   Skorko Glonek, Joanna ^a   Lipinska, Barbara ^a  

^a UNIVERSITY OF GDA SK   (Poland)

^b JAGIELLONIAN UNIVERSITY   (Poland)

^c Department of Biochemistry   (Italy)

Author keywords

Acrylamide quenching; Fluorescence spectroscopy; HtrA protein; Protein structure; Structural change; Trp mutant

Indexed keywords

ACRYLAMIDE; SERINE; SERINE PROTEINASE; SERINE PROTEINASE HTRA; TRYPTOPHAN; UNCLASSIFIED DRUG;

ARTICLE; CHEMICAL STRUCTURE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CORRELATIONAL STUDY; ENZYME ACTIVATION; ESCHERICHIA COLI; FLUORESCENCE; LIQUID CULTURE; MONITORING; MUTANT; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; STEADY STATE; TEMPERATURE;

CIRCULAR DICHROISM; ESCHERICHIA COLI; HEAT-SHOCK PROTEINS; HEAT-SHOCK RESPONSE; PERIPLASMIC PROTEINS; PROTEIN CONFORMATION; PROTEIN DENATURATION; SERINE ENDOPEPTIDASES; SPECTROSCOPY, FOURIER TRANSFORM INFRARED;

ESCHERICHIA COLI;

EID: 70249134884     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2009.07.002     Document Type: Article

References (33)

1. Clausen T., Southan C., and Ehrmann M. The HtrA family of proteases: implications for protein composition and cell fate. Mol. Cell 10 (2002) 443-455
2. Sohn J., Grant R.A., and Sauer R.T. Allosteric activation of DegS, a stress sensor PDZ protease. Cell 131 (2007) 572-583
3. Li W., Srinivasula S.M., Chai J., Li P., Wu J.W., Zhang Z., Alnemri E.S., and Shi Y. Structural insights into the pro-apoptotic function of mitochondrial serine protease HtrA2/Omi. Nat. Struct. Biol. 9 (2002) 410-412
4. Spiess C., Beil A., and Ehrmann M. A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein. Cell 97 (1999) 339-347
5. Kim D.Y., Kim D.R., Ha S.C., Lokanath N.K., Lee C.J., Hwang H.Y., and Kim K.K. Crystal structure of the protease domain of a heat-shock protein HtrA from Thermotoga maritima. J. Biol. Chem. 278 (2003) 6543-6551
6. Kim D.Y., Kwon E., Shin Y.K., Kweon D..H., and Kim K.K. The mechanism of temperature- induced bacterial HtrA activation. J. Mol. Biol. 377 (2008) 410-420
7. Krojer T., Garrido-Franco M., Huber R., Ehrmann M., and Clausen T. Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine. Nature 416 (2002) 455-459
8. Krojer T., Sawa J., Schäfer E., Saibil H.R., Ehrmann M., and Clausen T. Structural basis for the regulated protease and chaperone function of DegP. Nature 453 (2008) 885-890
9. Tabor S., and Richardson C.C. A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes. Proc. Natl. Acad. Sci. U. S. A. 82 (1985) 1074-1078
10. Russel M., and Model P. Replacement of the fip gene of Escherichia coli by an inactive gene cloned on a plasmid. J. Bacteriol. 159 (1984) 1034-1039
11. Skórko-Glonek J., Wawrzynów A., Krzewski K., Kurpierz K., and Lipińska B. Site-directed mutagenesis of the HtrA (DegP) serine protease, whose proteolytic activity is indispensable for Escherichia coli survival at elevated temperatures. Gene 163 (1995) 47-52
12. Skórko-Glonek J., Sobiecka-Szkatuła A., and Lipińska B. Characterization of disulfide exchange between DsbA and HtrA proteins from Escherichia coli. Acta Biochim. Pol. 53 (2006) 585-589
13. Lipińska B., Żylicz M., and Georgopoulos C. The HtrA (DegP) protein, essential for Escherichia coli survival at high temperatures, is an endopeptidase. J. Bacteriol. 172 (1990) 1791-1797
14. Salomaa P., Schaleger L.L., and Long F.A. Solvent deuterium isotope effects on acid-base equilibria. J. Am. Chem. Soc. 86 (1964) 1-7
15. Tanfani F., Galeazzi T., Curatola G., Bertoli E., and Ferretti G. Reduced beta-strand content in apoprotein B-100 in smaller and denser low-density lipoprotein subclasses as probed by Fourier-transform infrared spectroscopy. Biochem. J. 322 (1997) 765-769
16. Meersman F., Smeller L., and Heremans K. Comparative Fourier transform infrared spectroscopy study of cold-, pressure-, and heat-induced unfolding and aggregation of myoglobin. Biophys. J. 82 (2002) 2635-2644
17. Zolese G., Falcioni G., Bertoli E., Galeazzi R., Wozniak M., Wypych Z., Gratton E., and Ambrosini A. Steady-state and time resolved fluorescence of albumins interacting with N-oleylethanolamine, a component of the endogenous N-acylethanolamines. Proteins 40 (2000) 39-48
18. Kelly S.M., Jess T.J., and Price N.C. How to study proteins by circular dichroism. Biochim. Biophys. Acta 1751 (2005) 119-139
19. Eftink M.R., and Ghiron C.A. On the analysis of the temperature and viscosity dependence of fluorescence-quenching reactions with proteins. Arch. Biochem. Biophys. 209 (1981) 706-709
20. Stryjewski W., and Wasylewski Z. The resolution of heterogeneous fluorescence of multitryptophan-containing proteins studied by a fluorescence-quenching method. Eur. J. Biochem. 158 (1986) 547-553
21. Skórko-Glonek J., Krzewski K., Lipińska B., Bertoli E., and Tanfani F. Comparison of the structure of wild-type HtrA heat shock protease and mutant HtrA proteins. A Fourier transform infrared spectroscopic study. J. Biol. Chem. 270 (1995) 11140-11146
22. Arrondo J.L., Muga A., Castresana J., and Goni F.M. Quantitative studies of the structure of proteins in solution by Fourier-transform infrared spectroscopy. Prog. Biophys. Mol. Biol. 59 (1993) 23-56
23. Banuelos S., Arrondo J.L., Goni F.M., and Pifat G. Surface-core relationships in human low density lipoprotein as studied by infrared spectroscopy. J. Biol. Chem. 270 (1995) 9192-9196
24. Krimm S., and Bandekar J. Vibrational spectroscopy and conformation of peptides, polypeptides, and proteins. Adv. Protein Chem. 38 (1986) 181-364
25. Barth A., and Zscherp C. What vibrations tell us about proteins. Q. Rev. Biophys. 35 (2002) 369-430
26. Tanfani F., Scire A., Masullo M., Raimo G., Bertoli E., and Bocchini V. Salts induce structural changes in elongation factor 1alpha from the hyperthermophilic archaeon Sulfolobus solfataricus: a Fourier transform infrared spectroscopic study. Biochemistry 40 (2001) 13143-13148
27. Scirè A., Saccucci F., Bertoli E., Cambria M.T., Principato G., D'Auria S., and Tanfani F. Effect of acidic phospholipids on the structural properties of recombinant cytosolic human glyoxalase II. Proteins 48 (2002) 126-133
28. Kay E., Strickland E.H., and Billups C. Near ultraviolet circular dichroism and absorption spectra of chicken ovomucoid and acetylated derivatives at 297 and 77 degrees K. J. Biol. Chem. 249 (1974) 797-802
29. Cree D. The photophysics and photochemistry of the near-UV absorbing amino acids: I. Tryptophan and its simple derivatives. Photochem. Photobiol. 39 (1984) 537-562
30. Merrill A.R., Palmer L.R., and Szabo A.G. Acrylamide quenching of the intrinsic fluorescence of tryptophan residues genetically engineered into the soluble colicin E1 channel peptide. Structural characterization of the insertion-competent state. Biochemistry 32 (1993) 6974-6981
31. Mátyus L., Szöllosi J., and Jenei A. Steady-state fluorescence quenching applications for studying protein structure and dynamics. J. Photochem. Photobiol. B. 83 (2006) 223-236
32. Calhoun D.B., Vanderkooi J.M., Holtom G.R., and Englander S.W. Protein fluorescence quenching by small molecules: protein penetration versus solvent exposure. Proteins 1 (1986) 109-115
33. Lakowicz J.R. Principles of Fluorescence Spectroscopy (1999), Kluwer Academic/Plenum Publishers