دورية أكاديمية
أعرض في EDS

Evolution of the folding landscape of effector caspases.

التفاصيل البيبلوغرافية
العنوان: Evolution of the folding landscape of effector caspases.
المؤلفون: Shrestha S; Department of Biology, University of Texas at Arlington, Arlington, Texas, USA., Clark AC; Department of Biology, University of Texas at Arlington, Arlington, Texas, USA. Electronic address: clay.clark@uta.edu.
المصدر: The Journal of biological chemistry [J Biol Chem] 2021 Nov; Vol. 297 (5), pp. 101249. Date of Electronic Publication: 2021 Sep 28.
نوع المنشور: Journal Article; Research Support, N.I.H., Extramural
اللغة: English
بيانات الدورية: Publisher: Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology Country of Publication: United States NLM ID: 2985121R Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1083-351X (Electronic) Linking ISSN: 00219258 NLM ISO Abbreviation: J Biol Chem Subsets: MEDLINE
أسماء مطبوعة: Publication: 2021- : [New York, NY] : Elsevier Inc. on behalf of American Society for Biochemistry and Molecular Biology
Original Publication: Baltimore, MD : American Society for Biochemistry and Molecular Biology
مواضيع طبية MeSH: Evolution, Molecular* , Models, Molecular* , Protein Folding* , Protein Multimerization*, Caspases, Effector/*chemistry, Caspases, Effector/genetics ; Caspases, Effector/metabolism ; Humans
مستخلص: Caspases are a family of cysteinyl proteases that control programmed cell death and maintain homeostasis in multicellular organisms. The caspase family is an excellent model to study protein evolution because all caspases are produced as zymogens (procaspases [PCPs]) that must be activated to gain full activity; the protein structures are conserved through hundreds of millions of years of evolution; and some allosteric features arose with the early ancestor, whereas others are more recent evolutionary events. The apoptotic caspases evolved from a common ancestor (CA) into two distinct subfamilies: monomers (initiator caspases) or dimers (effector caspases). Differences in activation mechanisms of the two subfamilies, and their oligomeric forms, play a central role in the regulation of apoptosis. Here, we examine changes in the folding landscape by characterizing human effector caspases and their CA. The results show that the effector caspases unfold by a minimum three-state equilibrium model at pH 7.5, where the native dimer is in equilibrium with a partially folded monomeric (PCP-7, CA) or dimeric (PCP-6) intermediate. In comparison, the unfolding pathway of PCP-3 contains both oligomeric forms of the intermediate. Overall, the data show that the folding landscape was first established with the CA and was retained for >650 million years. Partially folded monomeric or dimeric intermediates in the ancestral ensemble provide mechanisms for evolutionary changes that affect stability of extant caspases. The conserved folding landscape allows for the fine-tuning of enzyme stability in a species-dependent manner while retaining the overall caspase-hemoglobinase fold.
Competing Interests: Conflict of interest The authors declare that they have no conflicts of interest with the contents of this article.
(Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved.)
References: Biochem J. 2019 Nov 29;476(22):3475-3492. (PMID: 31675069)
Proteins. 2002 Mar 1;46(4):355-67. (PMID: 11835511)
Mol Biol Evol. 2012 May;29(5):1353-66. (PMID: 22144639)
Cold Spring Harb Perspect Biol. 2013 Apr 01;5(4):a008656. (PMID: 23545416)
J Biol Chem. 2006 Mar 31;281(13):8667-74. (PMID: 16446367)
PLoS One. 2007 May 16;2(5):e446. (PMID: 17505540)
Biochemistry. 2013 Sep 10;52(36):6219-31. (PMID: 23941397)
Biochem J. 2004 Dec 1;384(Pt 2):201-32. (PMID: 15450003)
PLoS One. 2014 Oct 17;9(10):e110539. (PMID: 25330111)
ACS Chem Biol. 2016 Jun 17;11(6):1603-12. (PMID: 27032039)
Protein Sci. 2009 Dec;18(12):2500-17. (PMID: 19798740)
Arch Biochem Biophys. 2013 Mar;531(1-2):44-64. (PMID: 23246784)
J Biol Chem. 2020 Oct 23;295(43):14578-14591. (PMID: 32788218)
Chem Rev. 2016 Jun 8;116(11):6666-706. (PMID: 26750439)
J Mol Biol. 2002 Feb 15;316(2):327-40. (PMID: 11851342)
Proc Natl Acad Sci U S A. 2013 Jul 23;110(30):E2821-8. (PMID: 23836639)
Nucleic Acids Res. 2021 Jul 2;49(W1):W559-W566. (PMID: 34019657)
Genes Dev. 2013 Sep 15;27(18):2039-48. (PMID: 24065769)
J Biol Chem. 2001 Mar 9;276(10):7320-6. (PMID: 11058599)
Methods Enzymol. 2014;544:215-49. (PMID: 24974292)
Proc Natl Acad Sci U S A. 2010 Nov 23;107(47):20352-7. (PMID: 21048085)
Proc Natl Acad Sci U S A. 2016 Nov 15;113(46):13045-13050. (PMID: 27799545)
Nat Cell Biol. 2000 Jun;2(6):318-25. (PMID: 10854321)
Adv Exp Med Biol. 2012;747:55-73. (PMID: 22949111)
Protein Sci. 2018 Oct;27(10):1857-1870. (PMID: 30076665)
J Biol Chem. 2018 Apr 13;293(15):5447-5461. (PMID: 29414778)
Biopolymers. 2018 Aug;109(8):e23086. (PMID: 29152711)
Nature. 2020 May;581(7809):480-485. (PMID: 32461643)
Biochemistry. 2006 Nov 7;45(44):13249-63. (PMID: 17073446)
Proc Natl Acad Sci U S A. 2019 Apr 2;116(14):6806-6811. (PMID: 30877249)
Proc Natl Acad Sci U S A. 2016 Oct 11;113(41):E6080-E6088. (PMID: 27681633)
Biochemistry. 2001 Nov 27;40(47):14236-42. (PMID: 11714277)
Methods Enzymol. 2009;455:1-39. (PMID: 19289201)
J Biol Chem. 2016 Aug 12;291(33):17450-66. (PMID: 27325699)
Biochemistry. 2001 Nov 27;40(47):14224-35. (PMID: 11714276)
Proc Natl Acad Sci U S A. 1996 Jan 23;93(2):654-8. (PMID: 8570610)
Cell Chem Biol. 2019 Sep 19;26(9):1295-1305.e6. (PMID: 31353319)
Biochemistry. 2013 May 21;52(20):3415-27. (PMID: 23614869)
Proc Natl Acad Sci U S A. 2012 Nov 20;109(47):19244-9. (PMID: 23129648)
Nat Rev Mol Cell Biol. 2007 Apr;8(4):319-30. (PMID: 17356578)
Methods Enzymol. 2009;466:549-65. (PMID: 21609876)
Protein Expr Purif. 2012 Aug;84(2):236-46. (PMID: 22683476)
Protein Sci. 2016 Nov;25(11):2076-2088. (PMID: 27577093)
J Phys Chem Lett. 2015 Jun 4;6(11):2022-6. (PMID: 26266496)
Protein Sci. 2005 Jan;14(1):24-36. (PMID: 15576551)
Proc Natl Acad Sci U S A. 2013 May 21;110(21):8477-82. (PMID: 23650375)
Biochemistry. 2003 Oct 28;42(42):12298-310. (PMID: 14567691)
J Mol Biol. 2019 Dec 6;431(24):4796-4816. (PMID: 31520601)
Nat Rev Genet. 2013 Aug;14(8):559-71. (PMID: 23864121)
J Biol Chem. 2019 Jan 4;294(1):71-88. (PMID: 30420425)
Prog Biophys Mol Biol. 2008 Sep;98(1):61-84. (PMID: 18602415)
معلومات مُعتمدة: R01 GM127654 United States GM NIGMS NIH HHS
فهرسة مساهمة: Keywords: apoptosis; caspase; evolution; evolutionary biology; folding landscape; oligomerization; protease; protein evolution; protein folding
المشرفين على المادة: EC 3.4.22.- (Caspases, Effector)
تواريخ الأحداث: Date Created: 20210930 Date Completed: 20211215 Latest Revision: 20211215
رمز التحديث: 20231215
مُعرف محوري في PubMed: PMC8628267
DOI: 10.1016/j.jbc.2021.101249
PMID: 34592312
قاعدة البيانات: MEDLINE
الوصف
تدمد:1083-351X
DOI:10.1016/j.jbc.2021.101249