دورية أكاديمية
أعرض في EDS

HspB5 Chaperone Structure and Activity Are Modulated by Chemical-Scale Interactions in the ACD Dimer Interface.

التفاصيل البيبلوغرافية
العنوان: HspB5 Chaperone Structure and Activity Are Modulated by Chemical-Scale Interactions in the ACD Dimer Interface.
المؤلفون: Wang C; Program in Biochemistry, Mount Holyoke College, South Hadley, MA 01075, USA., Teng L; Program in Biochemistry, Mount Holyoke College, South Hadley, MA 01075, USA., Liu ZS; Program in Biochemistry, Mount Holyoke College, South Hadley, MA 01075, USA., Kamalova A; Program in Neuroscience and Behavior, Mount Holyoke College, South Hadley, MA 01075, USA., McMenimen KA; Program in Biochemistry, Mount Holyoke College, South Hadley, MA 01075, USA.; Program in Neuroscience and Behavior, Mount Holyoke College, South Hadley, MA 01075, USA.; Department of Chemistry, Mount Holyoke College, South Hadley, MA 01075, USA.
المصدر: International journal of molecular sciences [Int J Mol Sci] 2023 Dec 29; Vol. 25 (1). Date of Electronic Publication: 2023 Dec 29.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: MDPI Country of Publication: Switzerland NLM ID: 101092791 Publication Model: Electronic Cited Medium: Internet ISSN: 1422-0067 (Electronic) Linking ISSN: 14220067 NLM ISO Abbreviation: Int J Mol Sci Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Basel, Switzerland : MDPI, [2000-
مواضيع طبية MeSH: alpha-Crystallins*/genetics , Heat-Shock Proteins, Small*, Humans ; Biological Assay ; Molecular Chaperones/genetics ; Protein Folding
مستخلص: Small heat shock proteins (sHsps) are a family of ATP-independent molecular chaperones that function as "holdases" and prevent protein aggregation due to changes in temperature, pH, or oxidation state. sHsps have a conserved α-crystallin domain (ACD), which forms the dimer building block, flanked by variable N- and C-terminal regions. sHsps populate various oligomeric states as a function of their sequestrase activity, and these dynamic structural features allow the proteins to interact with a plethora of cellular substrates. However, the molecular mechanisms of their dynamic conformational assembly and the interactions with various substrates remains unclear. Therefore, it is important to gain insight into the underlying physicochemical properties that influence sHsp structure in an effort to understand their mechanism(s) of action. We evaluated several disease-relevant mutations, D109A, F113Y, R116C, R120G, and R120C, in the ACD of HspB5 for changes to in vitro chaperone activity relative to that of wildtype. Structural characteristics were also evaluated by ANS fluorescence and CD spectroscopy. Our results indicated that mutation Y113F is an efficient holdase, while D109A and R120G, which are found in patients with myofibrillar myopathy and cataracts, respectively, exhibit a large reduction in holdase activity in a chaperone-like light-scattering assay, which indicated alterations in substrate-sHsp interactions. The extent of the reductions in chaperone activities are different among the mutants and specific to the substrate protein, suggesting that while sHsps are able to interact with many substrates, specific interactions provide selectivity for some substrates compared to others. This work is consistent with a model for chaperone activity where key electrostatic interactions in the sHsp dimer provide structural stability and influence both higher-order sHsp interactions and facilitate interactions with substrate proteins that define chaperone holdase activity.
References: Front Mol Biosci. 2022 Feb 25;9:842149. (PMID: 35281256)
Cell Stress Chaperones. 2017 Jul;22(4):493-502. (PMID: 28120291)
Proc Natl Acad Sci U S A. 2013 Oct 1;110(40):E3780-9. (PMID: 24043785)
Biopolymers. 2007 Jun 15;86(3):177-92. (PMID: 17345631)
Nature. 1998 Aug 6;394(6693):595-9. (PMID: 9707123)
Annu Rev Microbiol. 2019 Sep 8;73:89-110. (PMID: 31091419)
PLoS One. 2014 Aug 26;9(8):e105892. (PMID: 25157403)
J Biol Chem. 2005 Feb 25;280(8):6337-48. (PMID: 15545279)
FASEB J. 2010 Oct;24(10):3633-42. (PMID: 20501794)
PLoS One. 2015 May 11;10(5):e0126761. (PMID: 25961584)
Annu Rev Biochem. 2009;78:959-91. (PMID: 19298183)
J Biol Chem. 2017 Jun 16;292(24):9944-9957. (PMID: 28487364)
Structure. 2015 Nov 3;23(11):2066-75. (PMID: 26439766)
Cell Stress Chaperones. 2020 Jul;25(4):573-580. (PMID: 32270443)
Cell Mol Life Sci. 2002 Oct;59(10):1649-57. (PMID: 12475175)
Nat Commun. 2016 Nov 30;7:13673. (PMID: 27901028)
J Mol Biol. 2023 Jul 1;435(13):168139. (PMID: 37146746)
Mol Vis. 2011;17:2356-67. (PMID: 21921988)
Int J Mol Sci. 2014 Dec 05;15(12):22518-38. (PMID: 25490136)
Biochem Biophys Res Commun. 2015 Mar 6;458(2):429-34. (PMID: 25660449)
Biochim Biophys Acta. 2016 Jan;1860(1 Pt B):240-5. (PMID: 26341790)
J Biol Chem. 2007 Nov 23;282(47):34276-87. (PMID: 17897943)
J Biol Chem. 2006 Dec 29;281(52):40420-8. (PMID: 17079234)
J Mol Biol. 2007 Sep 14;372(2):470-84. (PMID: 17662998)
Neuromuscul Disord. 2012 Jan;22(1):66-72. (PMID: 21920752)
Cell Stress Chaperones. 2020 Jul;25(4):655-665. (PMID: 32301006)
Elife. 2015 May 11;4:. (PMID: 25962097)
Curr Protein Pept Sci. 2012 Feb;13(1):76-85. (PMID: 22044147)
J Neurosci. 2011 Oct 26;31(43):15320-8. (PMID: 22031878)
FEBS Lett. 2007 Jul 31;581(19):3665-74. (PMID: 17467701)
J Mol Biol. 2009 Feb 6;385(5):1481-97. (PMID: 19041879)
Int J Mol Sci. 2023 Jan 06;24(2):. (PMID: 36674601)
Neurology. 2008 Nov 18;71(21):1660-8. (PMID: 18832141)
Cell Mol Life Sci. 2009 Jan;66(1):62-81. (PMID: 18810322)
Adv Exp Med Biol. 2020;1243:53-68. (PMID: 32297211)
EMBO J. 2012 Dec 12;31(24):4587-94. (PMID: 23188086)
J Cell Biol. 2011 Nov 14;195(4):617-29. (PMID: 22065637)
J Biol Chem. 2016 Oct 21;291(43):22618-22629. (PMID: 27587396)
Protein Sci. 2012 Jan;21(1):122-33. (PMID: 22057845)
Biochemistry (Mosc). 2012 Dec;77(13):1500-14. (PMID: 23379525)
Cell Stress Chaperones. 2017 Jul;22(4):577-588. (PMID: 28389817)
Proc Natl Acad Sci U S A. 2023 Feb 7;120(6):e2213765120. (PMID: 36719917)
Cell Stress Chaperones. 2010 Jul;15(4):457-61. (PMID: 19921466)
Biochemistry. 2015 Jul 21;54(28):4276-84. (PMID: 26098708)
Proteins. 2019 May;87(5):401-415. (PMID: 30684363)
BBA Clin. 2016 Nov 11;7:1-7. (PMID: 27904835)
Cell Stress Chaperones. 2017 Jul;22(4):601-611. (PMID: 28364346)
Biochem J. 2007 Jan 1;401(1):129-41. (PMID: 16928191)
EMBO J. 2021 Apr 15;40(8):e103811. (PMID: 33644875)
J Biol Chem. 2001 Oct 26;276(43):39945-9. (PMID: 11522798)
Biochemistry. 2009 Jan 20;48(2):442-53. (PMID: 19140694)
Nat Struct Mol Biol. 2010 Sep;17(9):1037-42. (PMID: 20802487)
Pharm Res. 2008 Jul;25(7):1487-99. (PMID: 18172579)
Cell Stress Chaperones. 2017 Jul;22(4):503-515. (PMID: 28130664)
Biochim Biophys Acta Proteins Proteom. 2017 May;1865(5):604-618. (PMID: 28179137)
J Mol Biol. 2009 Oct 9;392(5):1242-52. (PMID: 19646995)
Biochem Biophys Res Commun. 2006 Apr 7;342(2):379-86. (PMID: 16483541)
Mol Cell. 2015 Mar 5;57(5):836-849. (PMID: 25620563)
Science. 2016 Jul 1;353(6294):aac4354. (PMID: 27365453)
Cell Stress Chaperones. 2017 Jul;22(4):455-466. (PMID: 27933579)
Nat Struct Biol. 2001 Dec;8(12):1025-30. (PMID: 11702068)
J Biol Chem. 2019 Feb 8;294(6):2121-2132. (PMID: 30385502)
Proc Natl Acad Sci U S A. 2020 Feb 11;117(6):2923-2929. (PMID: 31974309)
Elife. 2019 Oct 01;8:. (PMID: 31573509)
Philos Trans R Soc Lond B Biol Sci. 2013 Mar 25;368(1617):20120327. (PMID: 23530263)
Nat Genet. 1998 Sep;20(1):92-5. (PMID: 9731540)
Protein Sci. 2010 May;19(5):1031-43. (PMID: 20440841)
J Struct Biol. 2012 Aug;179(2):152-60. (PMID: 22580344)
Philos Trans R Soc Lond B Biol Sci. 2013 Mar 25;368(1617):20110409. (PMID: 23530259)
J Struct Biol. 2011 Apr;174(1):92-9. (PMID: 21195185)
J Mol Biol. 2015 Apr 10;427(7):1537-48. (PMID: 25681016)
J Mol Biol. 1999 Jun 4;289(2):397-411. (PMID: 10366513)
Cell Stress Chaperones. 2017 Jul;22(4):569-575. (PMID: 28332148)
FEBS Lett. 2013 Apr 17;587(8):1073-80. (PMID: 23340341)
Langmuir. 2007 Feb 27;23(5):2714-21. (PMID: 17249699)
Biochimie. 2023 May;208:56-65. (PMID: 36521577)
Nat Struct Mol Biol. 2005 Oct;12(10):842-6. (PMID: 16205709)
Proc Natl Acad Sci U S A. 2009 Aug 11;106(32):13272-7. (PMID: 19651604)
J Mol Biol. 2020 Apr 17;432(9):3033-3049. (PMID: 32081587)
Cell Stress Chaperones. 2022 Jul;27(4):309-323. (PMID: 35678958)
Science. 2015 Nov 6;350(6261):674-7. (PMID: 26542570)
J Biol Chem. 2005 Jun 24;280(25):23869-75. (PMID: 15845535)
J Biol Chem. 2010 Apr 23;285(17):12778-86. (PMID: 20178975)
J Biol Chem. 2003 May 16;278(20):18015-21. (PMID: 12637495)
J Mol Biol. 2004 Oct 15;343(2):445-55. (PMID: 15451672)
J Struct Biol. 2014 Mar;185(3):342-54. (PMID: 24382496)
Cell Stress Chaperones. 2023 Nov;28(6):621-629. (PMID: 37462824)
Biochim Biophys Acta. 2014 Oct;1844(10):1808-19. (PMID: 25091198)
Cell Stress Chaperones. 2019 Mar;24(2):295-308. (PMID: 30758704)
J Biol Chem. 2013 Feb 15;288(7):4819-30. (PMID: 23277356)
Proc Natl Acad Sci U S A. 1999 May 25;96(11):6137-42. (PMID: 10339554)
J Biol Chem. 2004 Jan 09;279(2):1080-9. (PMID: 14573605)
Mol Cell. 2010 Oct 22;40(2):253-66. (PMID: 20965420)
Biochem Biophys Res Commun. 2007 Feb 23;353(4):1115-20. (PMID: 17207466)
J Biol Chem. 2004 Jul 30;279(31):32674-83. (PMID: 15152007)
EMBO J. 2015 Mar 12;34(6):778-97. (PMID: 25672362)
Mol Cell. 2018 Jan 18;69(2):214-226. (PMID: 29351843)
J Mol Biol. 2011 Apr 22;408(1):118-34. (PMID: 21329698)
معلومات مُعتمدة: R15 GM120654 United States GM NIGMS NIH HHS; R15GM120654-01 United States GM NIGMS NIH HHS
فهرسة مساهمة: Keywords: aggregation; chaperone; disease; mutations; protein misfolding; small heat shock proteins
المشرفين على المادة: 0 (alpha-Crystallins)
0 (Heat-Shock Proteins, Small)
0 (Molecular Chaperones)
0 (CRYAB protein, human)
تواريخ الأحداث: Date Created: 20240111 Date Completed: 20240116 Latest Revision: 20240210
رمز التحديث: 20240210
مُعرف محوري في PubMed: PMC10778692
DOI: 10.3390/ijms25010471
PMID: 38203641
قاعدة البيانات: MEDLINE
الوصف
تدمد:1422-0067
DOI:10.3390/ijms25010471