Folding and assembly kinetics of procaspase-3

Protein Science

Volumn 18, Issue 12, 2009, Pages 2500-2517

  Milam, Sara L ^a,b   Clark, A Clay ^a  

^a NORTH CAROLINA STATE UNIVERSITY   (United States)

^b DUKE UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

Apoptosis; Burst phase kinetics; Dimer assembly; Kinetic trap

Indexed keywords

ACRYLAMIDE; PROCASPASE 3;

ANISOTROPY; ARTICLE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; DIMERIZATION; DISSOCIATION; ENZYME CONFORMATION; FLUORESCENCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN FOLDING;

CASPASE 3; CIRCULAR DICHROISM; DIMERIZATION; ENZYME ACTIVATION; MODELS, MOLECULAR; PROTEIN CONFORMATION; PROTEIN FOLDING; SPECTROMETRY, FLUORESCENCE;

EID: 73149121172     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.259     Document Type: Article

References (44)

1. Fersht AR (2008) From the first protein structures to our current knowledge of protein folding: delights and scepticisms. Nature Rev Mol Cell Biol 9:650-654.
2. Goodsell DS, Olson AJ (2000) Structural symmetry and protein function. Ann Rev Biophys Biomol Struct 29:105-154.
3. Rumfeldt JAO, Galvagnion C, Vassall KA, Meiering EM (2008) Conformational stability and folding mechanisms of dimeric proteins. Prog Biophys Mol Biol 98:61-84.
4. Fuentes-Prior P, Salvesen GS (2004) The protein structures that shape caspase activity, specificity activation, and inhibition. Biochem J 384:201-232.
5. MacKenzie SH, Clark AC (2008) Targeting cell death in tumors by activating caspases. Curr Cancer Drug Targets 8:98-109.
6. Muzio M, Stockwell BR, Stennicke H, Salvesen GS, Dixit VM (1998) An induced proximity model for capase-8 activation. J Biol Chem 273:2926-2930.
7. Pop C, Timmer J, Sperandio S, Salvesen GS (2006) The apoptosome activates caspase-9 by dimerization. Mol Cell 22:269-275.
8. Pop C, Chen Y-R, Smith B, Bose K, Bobay B, Tripathy A, Franzen S, Clark AC (2001) Removal of the pro-domain does not affect the conformation of the procaspase-3 dimer. Biochemistry 40:14224-14235.
9. Shi Y (2004) Caspase activation, inhibition, and reactivation: a mechanistic view. Protein Sci 13:1979-1987.
10. Bose K, Clark AC (2001) Dimeric procaspase-3 unfolds via a four-state equilibrium process. Biochemistry 40:14236-14242.
11. Bose K, Clark AC (2005) pH effects on the stability and dimerization of procaspase-3. Protein Sci 14:24-36.
12. Bose K, Pop C, Feeney B, Clark AC (2003) An uncleavable procaspase-3 mutant has a lower catalytic efficiency but an active site similar to that of mature caspase-3. Biochemistry 42:12298-12310.
13. Feeney B, Clark AC (2005) Reassembly of active caspase-3 is facilitated by the propeptide. J Biol Chem 280:39772-39785.
14. Parker MJ, Spencer J, Clarke AR (1995) An integrated kinetic analysis of intermediates and transition states in protein folding reactions. J Mol Biol 253:771-786.
15. Ferguson N, Capaldi AP, James R, Kleanthous C, Radford SE (1999) Rapid folding with and without populated intermediates in the homologous four-helix proteins Im7 and Im9. J Mol Biol 286:1597-1608.
16. Jackson SE, Ferscht AR (1991) Folding of chymotrypsin 2.2. Influence of proline isomerization on the folding kinetics and thermodynamic characterization of the transition state of folding. Biochemistry 30:10436-10443.
17. Capaldi AP, Ferguson SJ, Radford SE (1999) The Greek key protein apo-pseudoazurin folds through an obligate on-pathway intermediate. J Mol Biol 286:1621-1632.
18. Barshop BA, Wrenn RF, Frieden C (1983). Analysis of numerical methods for computer simulation of kinetic processes: development of KINSIM - a flexible, portable system. Anal Biochem 130:134-145.
19. Kiefhaber T, Quass R, Hahn U, Schmid FX (1990) Folding of ribonuclease T1. I. Existence of multiple unfolded states created by proline isomerization. Biochemistry 29:3053-3061.
20. Brandts JF, Halvorson HR, Brennan M (1975). Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues. Biochemistry 14:4953-4963.
21. Medema JP, Scaffidi C, Kischkel FC, Shevchenko A, Mann M, Krammer PH, Peter ME (1997) FLICE is activated by association with the CD95 death-inducing signaling complex (DISC). EMBO J 16:2794-2804.
22. Kischkel FC, Hellbardt S, Behrmann I, Germer M, Pawlita M, Krammer PH, Peter ME (1995) Cytotoxicity-dependent APO-1 (Fas/CD95)-associated proteins form a death-inducing signaling complex (DISC) with the receptor. EMBO J 14:5579-5588.
23. Boatright KM, Renatus M, Scott FL, Sperandio S, Shin H, Pedersen IM, Ricci J-E, Edris WA, Sutherlin DP, Green DR, Salvesen G (2003) A unified model for apical caspase activation. Mol Cell 11:529-541.
24. Pop C, Fitzgerald P, Green DR, Salvesen GS (2007) Role of proteolysis in caspase-8 activation and stabilization. Biochemistry 46:4398-4407.
25. Richardson JS, Richardson DC (2002) Natural b-sheet proteins use negative design to avoid edge-to-edge aggregation. Proc Natl Acad Sci USA 99:2754-2759.
26. Toth G, Murphy RF, Lovas S (2001) Stabilization of local structures by p-CH and aromatic-backbone amide interactions involving prolyl and aromatic residues. Protein Eng 14:543-547.
27. Bhattacharyya R, Chakrabarti P (2003) Stereospecific interactions of proline residues in protein structures and complexes. J Mol Biol 331:925-940.
28. Pop C, Feeney B, Tripathy A, Clark AC (2003) Mutations in the procaspase-3 dimer interface affect the activity of the zymogen. Biochemistry 42:12311-12320.
29. Walters J, Pop C, Scott FL, Drag M, Swartz P, Mattos C, Salvesen GS, Clark AC (2009) A constitutively active and uninhibitable caspase-3 zymogen efficiently induces apoptosis. Biochemical Journal, in press.
30. Clark AC, Raso SW, Sinclair JF, Ziegler MM, Chaffotte AF, Baldwin TO (1997) Kinetic machanism of luciferase subunit folding and assembly. Biochemistry 36:1891-1899.
31. Milla ME, Sauer RT (1994) P22 Arc repressor: folding kinetics of a single-domain, dimeric protein. Biochemistry 33:1125-1133.
32. Ponstingl H, Kabir T, Gorse D, Thornton JM (2005) Morphological aspects of oligomeric protein structures. Prog Biophys Mol Biol 89:9-35.
33. Pontius BW (1993) Close encounters: why unstructured, polymeric domains can increase rates of specific macromolecular association. TIBS 18:181-186.
34. Michaeu O, Thome M, Schneider P, Holler N, Tschopp J, Nicholson DW, Briand C, Grutter MG (2002) The long form of FLIP is an activator of caspase-8 at the Fas death-inducing signaling complex. J Biol Chem 277:45162-45171.
35. Dohrman A, Russell S, Cuenin S, Fortner K, Tschopp J, Budd RC (2005) Cellular FLIP long form augments caspase activity and death of T cells through heterodimerization with and activation of caspase-8. J Immunol 175:311-318.
36. Yu JW, Jeffrey PD, Shi Y (2009). Mechanism of procaspase-8 activation by c-FLIPL. Proc Natl Acad Sci USA 106:8169-8174.
37. Riedl SJ, Fuentes-Prior P, Renatus M, Kairies N, Krapp S, Huber R, Salvesen GS, Bode W (2001). Structural basis for the activation of human procaspase-7. Proc Natl Acad Sci USA 98:14790-14795.
38. Chai J, Wu Q, Shiozaki E, Srinivasula SM, Alnemri ES, Shi Y (2001) Crystal structure of a procaspase-7 zymogen: mechanisms of activation and substrate binding. Cell 107:399-407.
39. Scott FL, Denault J-B, Riedl SJ, Shin H, Renatus M, Salvesen GS (2005) XIAP inhibits caspase-3 and -7 using two binding sites: evolutionarily conserved mechanism of IAPs. EMBO J 24:645-655.
40. MacCorkle RA, Freeman KW, Spencer DM (1998) Synthetic activation of caspases: artificial death switches. Proc Natl Acad Sci USA 95:3655-3660.
41. Jia L-T, Zhang L-H, Yu C-J, Zhao J, Xu Y-M, Gui J-H, Jin M, Ji Z-L, Wen W-H, Wang C-J, Chen S-Y, Yang A-G (2003) Specific tumoricidal activity of a secreted proapoptotic protein consisting of HER2 antibody and constitutively active caspase-3. Cancer Res 63:3257-3262.
42. Xu Y-M, Wang L-F, Jia L-T, Qiu X-C, Zhao J, Yu C-J, Zhang R, Zhu F, Wang C-J, Jin B-Q, Chen S-Y, Yang A-G (2004) A caspase-6 and anti-human epidermal growth factor receptor-2 (HER2) antibody chimeric molecule suppresses the growth of HER2-overexpressing tumors. J Immunol 173:61-67.
43. Pace CN (1986) Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol 131:266-280.
44. Walters J, Milam SL, Clark AC (2009) Practical approaches to protein folding and assembly: spectroscopic strategies in thermodynamics and kinetics. Methods Enzymol 455:1-39.