دورية أكاديمية
أعرض في EDS

Synonymous and non-synonymous codon substitutions can alleviate dependence on GroEL for folding.

التفاصيل البيبلوغرافية
العنوان: Synonymous and non-synonymous codon substitutions can alleviate dependence on GroEL for folding.
المؤلفون: Reingewertz TH; Department of Chemical and Structural Biology, Weizmann Institute of Science, Rehovot, Israel., Ben-Maimon M; Department of Chemical and Structural Biology, Weizmann Institute of Science, Rehovot, Israel., Zafrir Z; Department of Biomedical Engineering, Tel Aviv University, Tel Aviv, Israel., Tuller T; Department of Biomedical Engineering, Tel Aviv University, Tel Aviv, Israel.; The Sagol School of Neuroscience, Tel-Aviv University, Tel Aviv, Israel., Horovitz A; Department of Chemical and Structural Biology, Weizmann Institute of Science, Rehovot, Israel.
المصدر: Protein science : a publication of the Protein Society [Protein Sci] 2024 Aug; Vol. 33 (8), pp. e5087.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Cold Spring Harbor Laboratory Press Country of Publication: United States NLM ID: 9211750 Publication Model: Print Cited Medium: Internet ISSN: 1469-896X (Electronic) Linking ISSN: 09618368 NLM ISO Abbreviation: Protein Sci Subsets: MEDLINE
أسماء مطبوعة: Publication: 2001- : Woodbury, NY : Cold Spring Harbor Laboratory Press
Original Publication: New York, N.Y. : Cambridge University Press, c1992-
مواضيع طبية MeSH: Protein Folding* , Chaperonin 60*/genetics , Chaperonin 60*/chemistry , Chaperonin 60*/metabolism , Tetrahydrofolate Dehydrogenase*/genetics , Tetrahydrofolate Dehydrogenase*/chemistry , Tetrahydrofolate Dehydrogenase*/metabolism , Codon*/genetics , Codon*/metabolism , Escherichia coli*/genetics , Escherichia coli*/metabolism, Animals ; Mice ; Silent Mutation
مستخلص: The Escherichia coli GroEL/ES chaperonin system facilitates protein folding in an ATP-driven manner. There are <100 obligate clients of this system in E. coli although GroEL can interact and assist the folding of a multitude of proteins in vitro. It has remained unclear, however, which features distinguish obligate clients from all the other proteins in an E. coli cell. To address this question, we established a system for selecting mutations in mouse dihydrofolate reductase (mDHFR), a GroEL interactor, that diminish its dependence on GroEL for folding. Strikingly, both synonymous and non-synonymous codon substitutions were found to reduce mDHFR's dependence on GroEL. The non-synonymous substitutions increase the rate of spontaneous folding whereas computational analysis indicates that the synonymous substitutions appear to affect translation rates at specific sites.
(© 2024 The Author(s). Protein Science published by Wiley Periodicals LLC on behalf of The Protein Society.)
References: Proc Natl Acad Sci U S A. 2006 Oct 24;103(43):15800-5. (PMID: 17043235)
BMC Genomics. 2015;16 Suppl 10:S4. (PMID: 26449467)
FEBS J. 2012 Feb;279(4):543-50. (PMID: 22177460)
Proc Natl Acad Sci U S A. 2010 Jun 29;107(26):11793-8. (PMID: 20547872)
Nucleic Acids Res. 2004 Sep 24;32(17):5036-44. (PMID: 15448185)
Nucleic Acids Res. 2013 Jan;41(Database issue):D36-42. (PMID: 23193287)
J Biol Chem. 2017 Dec 15;292(50):20583-20591. (PMID: 29066625)
EMBO J. 2010 May 5;29(9):1552-64. (PMID: 20360681)
Methods Mol Biol. 2014;1116:89-101. (PMID: 24395359)
FEBS Lett. 2009 Aug 20;583(16):2654-62. (PMID: 19577567)
Methods Enzymol. 1987;155:416-33. (PMID: 2828874)
Q Rev Biophys. 2014 Nov;47(4):285-363. (PMID: 25225856)
Proc Natl Acad Sci U S A. 2010 Feb 23;107(8):3645-50. (PMID: 20133581)
Commun Biol. 2021 May 17;4(1):589. (PMID: 34002016)
DNA Res. 2014 Oct;21(5):511-26. (PMID: 24906480)
Nature. 1998 Mar 12;392(6672):139. (PMID: 9515958)
J Mol Biol. 2020 Sep 18;432(20):5649-5664. (PMID: 32835659)
PLoS One. 2018 Feb 13;13(2):e0192619. (PMID: 29438383)
Trends Biochem Sci. 2016 Jan;41(1):62-76. (PMID: 26422689)
Biochemistry. 2021 Feb 16;60(6):460-464. (PMID: 33464880)
Nucleic Acids Res. 1987 Feb 11;15(3):1281-95. (PMID: 3547335)
Biophys J. 2019 Jan 8;116(1):42-48. (PMID: 30577980)
J Struct Biol. 2010 Oct;172(1):34-44. (PMID: 20600952)
Comput Struct Biotechnol J. 2021 Apr 22;19:2646-2663. (PMID: 34025951)
Nature. 1994 Oct 13;371(6498):578-86. (PMID: 7935790)
Genome Biol. 2020 Mar 9;21(1):63. (PMID: 32151272)
BMC Genomics. 2015;16 Suppl 10:S5. (PMID: 26449596)
Bioinformatics. 2020 Mar 1;36(5):1439-1444. (PMID: 31599925)
Biochem Cell Biol. 2010 Apr;88(2):185-94. (PMID: 20453921)
Mol Cell. 2017 Nov 2;68(3):515-527.e6. (PMID: 29100052)
Elife. 2020 Jul 27;9:. (PMID: 32716842)
Proc Natl Acad Sci U S A. 2014 Sep 2;111(35):12775-80. (PMID: 25136110)
FASEB J. 1996 Jan;10(1):5-9. (PMID: 8566548)
Nucleic Acids Res. 2009 Jan;37(Database issue):D93-7. (PMID: 18984615)
Genome Biol. 2011 Nov 03;12(11):R110. (PMID: 22050731)
Q Rev Biophys. 2020 Feb 19;53:e4. (PMID: 32070442)
Cell. 2014 May 8;157(4):922-934. (PMID: 24813614)
Protein Sci. 2005 Jan;14(1):193-201. (PMID: 15576562)
Nature. 2000 Oct 12;407(6805):757-62. (PMID: 11048724)
J Biol Chem. 2014 Nov 14;289(46):32073-32080. (PMID: 25288795)
Acc Chem Res. 2014 May 20;47(5):1536-44. (PMID: 24784899)
Cell. 2005 Jul 29;122(2):209-20. (PMID: 16051146)
Protein Sci. 2018 Jan;27(1):135-145. (PMID: 28884485)
Protein Sci. 1992 Mar;1(3):363-9. (PMID: 1363913)
Biochemistry. 1991 Oct 8;30(40):9716-23. (PMID: 1680394)
Biochemistry. 1990 May 29;29(21):5195-202. (PMID: 1974147)
RNA. 2015 Oct;21(10):1704-18. (PMID: 26246046)
RNA Biol. 2021 Dec;18(12):2296-2307. (PMID: 33691590)
FASEB J. 1990 May;4(8):2441-52. (PMID: 2185970)
Nucleic Acids Res. 2016 Jul 8;44(W1):W54-7. (PMID: 27174935)
Annu Rev Biophys. 2024 Jul;53(1):87-108. (PMID: 38134335)
J Biol Chem. 1991 Oct 25;266(30):19890-3. (PMID: 1939053)
Nature. 1997 Aug 21;388(6644):741-50. (PMID: 9285585)
FEBS Lett. 2016 Jan;590(2):251-7. (PMID: 26762164)
J Mol Biol. 1993 May 5;231(1):58-64. (PMID: 8098773)
Annu Rev Biophys. 2022 May 9;51:115-133. (PMID: 34982571)
Protein Sci. 2020 Feb;29(2):360-377. (PMID: 31800116)
معلومات مُعتمدة: Minerva Foundation with funding from the Federal German Ministry for Education and Research; 2021077 US-Israel Binational Science Foundation; Helen & Milton A. Kimmelman Center for Biomolecular Structure and Assembly; Ilse Katz Institute for Material Sciences and Magnetic Resonance Research
فهرسة مساهمة: Keywords: GroEL; chaperonins; codon usage; protein folding; random mutagenesis
المشرفين على المادة: 0 (Chaperonin 60)
EC 1.5.1.3 (Tetrahydrofolate Dehydrogenase)
0 (Codon)
تواريخ الأحداث: Date Created: 20240729 Date Completed: 20240729 Latest Revision: 20240731
رمز التحديث: 20240731
مُعرف محوري في PubMed: PMC11285870
DOI: 10.1002/pro.5087
PMID: 39074255
قاعدة البيانات: MEDLINE
الوصف
تدمد:1469-896X
DOI:10.1002/pro.5087