Thermal, Chemical and pH Induced Denaturation of a Multimeric β-Galactosidase Reveals Multiple Unfolding Pathways

PLoS ONE

Volumn 7, Issue 11, 2012, Pages

  Kishore, Devesh ^a   Kundu, Suman ^b   Kayastha, Arvind M ^a  

^a BANARAS HINDU UNIVERSITY   (India)

^b UNIVERSITY OF DELHI   (India)

Author keywords

[No Author keywords available]

Indexed keywords

BETA GALACTOSIDASE; GUANIDINE DERIVATIVE; GUANIDIUM HYDROCHLORIDE; UNCLASSIFIED DRUG; UREA;

ARTICLE; CHICKPEA; CIRCULAR DICHROISM; DIMERIZATION; ENERGY YIELD; ENZYME ACTIVITY; ENZYME DENATURATION; ENZYME STABILITY; ENZYME STRUCTURE; FLUORESCENCE SPECTROSCOPY; HIGH TEMPERATURE; MOLECULAR WEIGHT; PH; PROTEIN AGGREGATION; PROTEIN CONFORMATION; PROTEIN UNFOLDING; THERMODYNAMICS;

BETA-GALACTOSIDASE; CICER; CIRCULAR DICHROISM; GUANIDINE; HYDROGEN-ION CONCENTRATION; PLANT PROTEINS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN MULTIMERIZATION; PROTEIN STABILITY; PROTEIN UNFOLDING; SPECTROMETRY, FLUORESCENCE; TEMPERATURE; THERMODYNAMICS; UREA;

CICER ARIETINUM; KOBUS;

EID: 84869761065     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0050380     Document Type: Article

References (35)

1. Nichtl A, Buchner J, Jaenicke R, Rudolph R, Scheibel T, (1998) Folding and association of β-galactosidase. J Mol Biol 282: 1083-1091.
2. Kaplan J, DeGrado WF, (2004) De novo design of catalytic proteins. Proc Natl Acad Sci USA 101: 11566-11570.
3. Lassila JK, Privett HK, Allen BD, Mayo SL, (2006) Combinatorial methods for small-molecule placement in computational enzyme design. Proc Natl Acad Sci USA 103: 16710-16715.
4. Radford SE, (2000) Protein folding: progress made and promises ahead. Trends Biochem Sci 25: 611-618.
5. Jagannadham MV, Dubey VK, (2003) Differences in the unfolding of procerain induced by pH, guanidine hydrochloride, urea, and temperature. Biochemistry 42: 12287-12297.
6. Selkoe DJ, (2003) Folding proteins in fatal ways. Nature 426: 900-904.
7. Yadav SC, Jagannadham MV, (2009) Complete conformational stability of kinetically stable dimeric serine protease milin against pH, temperature, urea, and proteolysis. Eur Biophys J Biophy Lett 38: 981-991.
8. Duy C, Fitter J, (2006) How aggregation and conformational scrambling of unfolded states govern fluorescence emission spectra. Biophys J 90: 3704-3711.
9. Dill KA, Ozkan SB, Weikl TR, Chodera JD, Voelz VA, (2007) The protein folding problem: when will it be solved? Curr Opin Struct Biol 17: 342-346.
10. Pribila BA, Hertzler SR, Martin BR, Weaver CM, Savaiano DA, (2000) Improved lactose digestion and intolerance among African-American adolescent girls fed on a dairy-rich diet. J Am Diet Assoc 100: 524-528; quiz 529-530.
11. Kishore D, Kayastha AM, (2012) Optimization of immobilization conditions for chick pea β-galactosidase (CpGAL) to alkylamine glass using response surface methodology and its applications in lactose hydrolysis. Food Chem 134: 1650-1657.
12. Kishore D, Talat M, Srivastava ON, Kayastha AM, (2012) Immobilization of β-galactosidase onto functionalized graphene nano-sheets using response surface methodology and its analytical applications. PLoS ONE 7: e40708.
13. Casadaban MJ, Cohen SN, (1980) Analysis of gene control signals by DNA fusion and cloning in Escherichia coli. J Mol Biol 138: 179-207.
14. Nathan DF, Lindquist S, (1995) Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase. Mol Cell Biol 15: 3917-3925.
15. Kishore D, Kayastha AM, (2012) A β-galactosidase from chick pea (Cicer arietinum) seeds: Its purification, biochemical properties and industrial applications. Food Chem 134: 1113-1122.
16. Semisotnov GV, Rodionova NA, Razgulyaev OI, Uversky VN, Gripas AF, et al. (1991) Study of the molten globule intermediate state in protein folding by a hydrophobic fluorescent-probe. Biopolymers 31: 119-128.
17. Khurana R, Udgaonkar JB, (1994) Equilibrium unfolding studies of Barstar- Evidence for an alternative conformation which resembles a molten globule. Biochemistry 33: 106-115.
18. Bradford MM, (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
19. Greenfield NJ, (2006) Determination of the folding of proteins as a function of denaturants, osmolytes or ligands using circular dichroism. Nature Protoc 1: 2733-2741.
20. Manavalan P, Johnson WC, (1983) Sensitivity of circular-dichroism to protein tertiary structure class. Nature 305: 831-832.
21. Greenfield NJ, (2006) Using circular dichroism spectra to estimate protein secondary structure. Nat Protoc 1: 2876-2890.
22. Duy C, Fitter J, (2005) Thermostability of irreversible unfolding α-amylases analyzed by unfolding kinetics. J Biol Chem 280: 37360-37365.
23. Fitter J, Haber-Pohlmeier S, (2004) Structural stability and unfolding properties of thermostable bacterial α-amylases: a comparative study of homologous enzymes. Biochemistry 43: 9589-9599.
24. Vogl T, Jatzke C, Hinz HJ, Benz J, Huber R, (1997) Thermodynamic stability of annexin V E17G: equilibrium parameters from an irreversible unfolding reaction. Biochemistry 36: 1657-1668.
25. Lepock JR, Ritchie KP, Kolios MC, Rodahl AM, Heinz KA, et al. (1992) Influence of transition rates and scan rate on kinetic simulations of differential scanning calorimetry profiles of reversible and irreversible protein denaturation. Biochemistry 31: 12706-12712.
26. Benjwal S, Verma S, Rohm KH, Gursky O, (2006) Monitoring protein aggregation during thermal unfolding in circular dichroism experiments. Protein Sci 15: 635-639.
27. Yan YB, Wang Q, He HW, Zhou HM, (2004) Protein thermal aggregation involves distinct regions: sequential events in the heat-induced unfolding and aggregation of hemoglobin. Biophys J 86: 1682-1690.
28. Halfman CJ, Nishida T, (1971) Influence of pH and electrolyte on the fluorescence of bovine serum albumin. Biochimi Biophys Acta (BBA)- Protein Struct 243: 284-293.
29. Fitter J, (2003) A measurement of conformational entropy change during thermal protein unfolding using neutron spectroscopy. Biophysical J 84: 3924-3930.
30. Fink AL, Calciano LJ, Goto Y, Kurotsu T, Palleros DR, (1994) Classification of acid denaturation of proteins: intermediates and unfolded states. Biochemistry 33: 12504-12511.
31. Dwevedi A, Dubey VK, Jagannadham MV, Kayastha AM, (2010) Insights into pH-induced conformational transition of β-galactosidase from Pisum sativum leading to its multimerization. Appl Biochem Biotechnol 162: 2294-2312.
32. Wong KP, Tanford C, (1973) Denaturation of bovine carbonic anhydrase B by guanidine hydrochloride. A process involving separable sequential conformational transitions. J Biol Chem 248: 8518-8523.
33. Jacobson RH, Zhang XJ, DuBose RF, Matthews BW, (1994) Three-dimensional structure of β-galactosidase from E. coli. Nature 369: 761-766.
34. Sundd M, Kundu S, Jagannadham MV, (2002) Acid and chemical induced conformational changes of ervatamin B. Presence of partially structured multiple intermediates. J Biochem Mol Biol 35: 143-154.
35. Tripathi P, Hofmann H, Kayastha AM, Ulbrich-Hofmann R, (2008) Conformational stability and integrity of α-amylase from mung beans: evidence of kinetic intermediate in GdmCl-induced unfolding. Biophys Chem 137: 95-99.