Fluorescence study on interactions of α-crystallin with the molten globule state of 1, 4-β-D-glucan Glucanohydrolase from Thermomonospora sp. induced by guanidine hydrochloride

Journal of Fluorescence

Volumn 19, Issue 6, 2009, Pages 967-973

  Jagtap, Sharmili ^a   Rao, Mala ^a  

^a NATIONAL CHEMICAL LABORATORY   (India)

Author keywords

ANS; Cellulase; Guanidine hydrochloride; Protein folding

Indexed keywords

ANS; BINDING STUDIES; BIOLOGICAL ACTIVITIES; CHAPERONE ACTIVITY; CIRCULAR DICHROISM; CRYSTALLIN; FLUORESCENCE QUENCHING; FLUORESCENCE STUDIES; FOLDED STATE; GLUCOHYDROLASE; GUANIDINE HYDROCHLORIDE; IN-VITRO; INTRINSIC TRYPTOPHAN FLUORESCENCES; MOLECULAR MECHANISM; MOLTEN GLOBULE; MOLTEN GLOBULE STATE; PHYSIOLOGICAL CONDITION; REFOLDING; REFOLDING PATHWAYS; THREE-DIMENSIONAL FLUORESCENCE SPECTRA;

AMINO ACIDS; DICHROISM; ENZYME ACTIVITY; FLUORESCENCE; QUENCHING;

PROTEIN FOLDING;

ALPHA CRYSTALLIN; BACTERIAL PROTEIN; GLUCAN 1,4 BETA GLUCOSIDASE; GUANIDINE; TRYPTOPHAN;

ACTINOMYCETALES; ARTICLE; CHEMICAL MODEL; CHEMISTRY; CIRCULAR DICHROISM; FLUORESCENCE; HYDROPHOBICITY; METHODOLOGY; PROTEIN DENATURATION; PROTEIN FOLDING; SPECTROFLUOROMETRY; TEMPERATURE; TIME;

ACTINOMYCETALES; ALPHA-CRYSTALLINS; BACTERIAL PROTEINS; CIRCULAR DICHROISM; FLUORESCENCE; GLUCAN 1,4-BETA-GLUCOSIDASE; GUANIDINE; HYDROPHOBICITY; MODELS, CHEMICAL; PROTEIN DENATURATION; PROTEIN FOLDING; SPECTROMETRY, FLUORESCENCE; TEMPERATURE; TIME FACTORS; TRYPTOPHAN;

THERMOMONOSPORA;

EID: 72149095439     PISSN: 10530509     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10895-009-0496-5     Document Type: Article

References (25)

1. CB Anfinsen 1973 Principles that govern the folding of protein chains Science 181 223 230 10.1126/science.181.4096.223 10.1126/science.181.4096.223 1:CAS:528:DyaE3sXkvVygtbc%3D 4124164
2. R Jaenicke 1987 Folding and association of proteins Prog Biophys Mol Biol 49 117 237 10.1016/0079-6107(87)90011-3 10.1016/0079-6107(87)90011-3 1:CAS:528:DyaL1cXovFKksw%3D%3D 3327098
3. R Jaenicke R Rudolph 1986 Refolding and association of oligomeric proteins Methods Enzymol Enzyme Structure part L 131 218 250 10.1016/0076-6879(86)31043-7 1:CAS:528:DyaL2sXotVCiuw%3D%3D
4. M Arai K Kuwajima 2000 Role of the molten globule state in protein folding Adv Protein Chem 53 209 271 10.1016/S0065-3233(00)53005-8 10.1016/S0065-3233(00)53005-8 1:CAS:528:DC%2BD3cXlt1Oktbw%3D 10751946 Protein folding mechanisms (Pubitemid 34194295)
5. K Lang FX Schmid G Fisher 1987 Catalysis of protein folding by prolyl isomerase Nature 329 268 270 10.1038/329268a0 10.1038/329268a0 1:CAS:528:DyaL2sXmtlajsLs%3D 3306408 (Pubitemid 17128975)
6. JP Hendrick FU Hartl 1993 Molecular chaperone functions of heat-shock proteins Annu Rev Biochem 62 349 384 10.1146/annurev.bi.62.070193.002025 10.1146/annurev.bi.62.070193.002025 1:CAS:528:DyaK3sXlsFCjurw%3D 8102520
7. RJ Siezen P Argos 1983 Structural homology of lens crystallins. III. Secondary structure estimation from circular dichroism and prediction from amino acid sequences Biochim Biophys Acta 748 56 67 1:CAS:528:DyaL2cXitlyn 6615851
8. RV Montfort C Slingsby E Vierlingt 2001 Structure and function of the small heat shock protein/α-crystallin family of molecular chaperones Adv Protein Chem 59 105 156 10.1016/S0065-3233(01)59004-X 10.1016/S0065-3233(01) 59004-X 11868270 Protein folding in the cell (Pubitemid 34169303)
9. R Klemenz E Frohli RH Steiger R Schafer A Aoyama 1991 α B-Crystallin is a small heat shock protein Proc Natl Acad Sci USA 88 3652 3656 10.1073/pnas.88.9.3652 10.1073/pnas.88.9.3652 1:CAS:528:DyaK3MXktVenurg%3D 2023914
10. J Horwitz 1993 Proctor Lecture. The function of alpha-crystallin Invest Ophthalmol Vis Sci 34 10 21 1:STN:280:DyaK3s7ks1OrtQ%3D%3D 8425816
11. MJ Kelley I David N Iwasaki J Wright TR Shearer 1993 α-crystallin chaperone activity is reduced by calpain II in vitro and in selenite cataract J Biol Chem 268 18844 18849 1:CAS:528:DyaK3sXmtVWisL8%3D 8395520
12. GH Lorimer TO Baldwin 1998 Lens crystallin: chaperone like properties methods Enzymol Molecular Chaperones 290 365 384 10.1016/S0076-6879(98)90032-5 (Pubitemid 28157764)
13. B Raman CM Rao 1994 Chaperone-like activity and quaternary structure of alpha-crystallin J Biol Chem 269 27264 27268 1:CAS:528:DyaK2cXmt1Cmtb4%3D 7961635
14. PJ Groenen KB Merck WW de Jong H Bloemendal 1994 Structure and modifications of the junior chaperone alpha-crystallin: from lens transparency to molecular pathology Eur J Biochem 225 1 19 10.1111/j.1432-1033.1994.00001.x 10.1111/j.1432-1033.1994.00001.x 1:CAS:528:DyaK2cXlvFylsLY%3D 7925426 (Pubitemid 24306223)
15. U Jakob M Gaestel K Engel J Buchner 1993 Small heat shock proteins are molecular chaperones J Biol Chem 268 1517 1520 1:CAS:528:DyaK3sXitVOru7k%3D 8093612
16. S Jagtap M Rao 2005 Purification and properties of a low molecular weight 1, 4-β-D-Glucan glucohydrolase having one active site for carboxymethyl cellulose and xylan from an alkalothermophilic Thermomonospora sp Biochem Biophys Res Commun 329 111 116 10.1016/j.bbrc.2005.01.102 10.1016/j.bbrc.2005. 01.102 1:CAS:528:DC%2BD2MXhsFSju7k%3D 15721281 (Pubitemid 40255428)
17. S Jagtap M Rao 2006 Conformation and microenvironment of the active site of a low molecular weight 1,4-β-D-Glucan Glucanohydrolase from an alkalothermophilic Thermomonospora sp.: Involvement of a lysine and cysteine residue Biochem Biophys Res Commun 347 428 432 10.1016/j.bbrc.2006.06.100 10.1016/j.bbrc.2006.06.100 1:CAS:528:DC%2BD28XntFWktL4%3D 16828055 (Pubitemid 44041434)
18. AM Labhardt 1986 Folding intermediates studied by circular dichroism Methods Enzymol 131 126 135 10.1016/0076-6879(86)31038-3 10.1016/0076-6879(86) 31038-3 1:CAS:528:DyaL2sXotFSqsA%3D%3D 3773754
19. RL Baldwin 1986 Temperature dependence of the hydrophobic interaction in protein folding Proc Natl Acad Sci USA 83 8069 8072 10.1073/pnas.83.21.8069 10.1073/pnas.83.21.8069 1:CAS:528:DyaL2sXitVSk 3464944 (Pubitemid 17182445)
20. WK Surewicz PR Olesen 1995 On the thermal stability of alpha-crystallin: a new insight from infrared spectroscopy Biochemistry 34 9655 9660 10.1021/bi00030a001 10.1021/bi00030a001 1:CAS:528:DyaK2MXmvVeisro%3D 7626634
21. VE Bychkova RH Pain OB Ptitsyn 1988 The 'molten globule' state is involved in the translocation of proteins across membranes? FEBS Lett 238 231 234 10.1016/0014-5793(88)80485-X 10.1016/0014-5793(88)80485-X 1:CAS:528:DyaL1MXjsFCgsQ%3D%3D 3049159 (Pubitemid 18244924)
22. B Raman T Ramakrishna CM Rao 1997 Effect of the chaperone-like alpha-crystallin on the refolding of lysozyme and ribonuclease A FEBS Lett 416 369 372 10.1016/S0014-5793(97)01240-4 10.1016/S0014-5793(97)01240-4 1:CAS:528:DyaK2sXmvFWjsbY%3D 9373187 (Pubitemid 27475399)
23. KP Das JM Petrash WK Surewicz 1996 Conformational properties of substrate proteins bound to a molecular chaperone α-crystallin J Biol Chem 271 10449 10452 10.1074/jbc.271.28.16934 10.1074/jbc.271.28.16934 1:CAS:528:DyaK28XivVaqsLo%3D 8631839 (Pubitemid 26239064)
24. CN Pace 1986 Determination and analysis of urea and guanidine hydrochloride denaturation curves Methods Enzymol 131 266 280 10.1016/0076-6879(86)31045-0 10.1016/0076-6879(86)31045-0 1:CAS:528: DyaL2sXmtlOitw%3D%3D 3773761
25. TM Pakula M Laxell A Huuskonen J Uusitalo M Saloheimo M Penttilä 2003 The effects of drugs inhibiting protein secretion in the filamentous fungus Trichoderma reesei: evidence for down-regulation of genes that encode secreted proteins in the stressed cells J Biol Chem 278 45011 45020 10.1074/jbc. M302372200 10.1074/jbc.M302372200 1:CAS:528:DC%2BD3sXoslWlt7o%3D 12941955 (Pubitemid 37377261)