Structure and function of yeast Lso2 and human CCDC124 bound to hibernating ribosomes.

Tytuł:: Structure and function of yeast Lso2 and human CCDC124 bound to hibernating ribosomes.
Autorzy:: Wells JN; Gene Center and Center for Integrated Protein Science Munich, Department of Biochemistry, University of Munich, Munich, Germany.
Buschauer R; Gene Center and Center for Integrated Protein Science Munich, Department of Biochemistry, University of Munich, Munich, Germany.
Mackens-Kiani T; Gene Center and Center for Integrated Protein Science Munich, Department of Biochemistry, University of Munich, Munich, Germany.
Best K; Gene Center and Center for Integrated Protein Science Munich, Department of Biochemistry, University of Munich, Munich, Germany.
Kratzat H; Gene Center and Center for Integrated Protein Science Munich, Department of Biochemistry, University of Munich, Munich, Germany.
Berninghausen O; Gene Center and Center for Integrated Protein Science Munich, Department of Biochemistry, University of Munich, Munich, Germany.
Becker T; Gene Center and Center for Integrated Protein Science Munich, Department of Biochemistry, University of Munich, Munich, Germany.
Gilbert W; Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut, United States of America.
Cheng J; Gene Center and Center for Integrated Protein Science Munich, Department of Biochemistry, University of Munich, Munich, Germany.
Beckmann R; Gene Center and Center for Integrated Protein Science Munich, Department of Biochemistry, University of Munich, Munich, Germany.
Źródło:: PLoS biology [PLoS Biol] 2020 Jul 20; Vol. 18 (7), pp. e3000780. Date of Electronic Publication: 2020 Jul 20 (Print Publication: 2020).
Typ publikacji:: Journal Article; Research Support, Non-U.S. Gov't
Język:: English
Imprint Name(s):: Original Publication: San Francisco, CA : Public Library of Science, [2003]-
MeSH Terms:: Cell Cycle Proteins/*chemistry
Cell Cycle Proteins/*metabolism
Intracellular Signaling Peptides and Proteins/*chemistry
Intracellular Signaling Peptides and Proteins/*metabolism
Ribosomal Proteins/*chemistry
Ribosomal Proteins/*metabolism
Ribosomes/*metabolism
Saccharomyces cerevisiae/*metabolism
Saccharomyces cerevisiae Proteins/*chemistry
Saccharomyces cerevisiae Proteins/*metabolism
Adaptor Proteins, Signal Transducing/metabolism ; Amino Acid Sequence ; Binding Sites ; Conserved Sequence ; Evolution, Molecular ; HEK293 Cells ; Humans ; Models, Molecular ; Peptides/chemistry ; Protein Binding ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; RNA, Transfer/metabolism ; RNA-Binding Proteins/metabolism ; Ribosomes/ultrastructure ; Saccharomyces cerevisiae/ultrastructure ; Structure-Activity Relationship
References:: Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Sep 1;63(Pt 9):768-70. (PMID: 17768350)
Nature. 2004 Feb 26;427(6977):808-14. (PMID: 14985753)
J Cell Biol. 2010 Aug 23;190(4):613-21. (PMID: 20733057)
Proc Natl Acad Sci U S A. 2007 Dec 11;104(50):19671-8. (PMID: 18003906)
J Biol Chem. 2010 May 14;285(20):14848-14851. (PMID: 20356839)
Mol Cell. 2019 Mar 7;73(5):959-970.e5. (PMID: 30686592)
Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 1):2126-32. (PMID: 15572765)
Science. 2011 Dec 16;334(6062):1524-9. (PMID: 22096102)
J Biochem. 2008 Mar;143(3):425-33. (PMID: 18174192)
Nat Struct Mol Biol. 2012 Dec;19(12):1234-41. (PMID: 23142978)
Nat Commun. 2017 Sep 28;8(1):723. (PMID: 28959035)
Mol Biol Cell. 2000 Mar;11(3):833-48. (PMID: 10712503)
J Biol Chem. 2002 Apr 19;277(16):13848-55. (PMID: 11796711)
EMBO J. 2004 Mar 10;23(5):1008-19. (PMID: 14976550)
J Comput Chem. 2004 Oct;25(13):1605-12. (PMID: 15264254)
Proc Natl Acad Sci U S A. 2017 Sep 26;114(39):E8165-E8173. (PMID: 28894000)
J Struct Biol. 2016 Jan;193(1):1-12. (PMID: 26592709)
Science. 1997 Dec 19;278(5346):2123-6. (PMID: 9405348)
J Cell Physiol. 2018 Dec;233(12):9110-9120. (PMID: 30076717)
Acta Crystallogr D Biol Crystallogr. 2010 Jan;66(Pt 1):12-21. (PMID: 20057044)
EMBO J. 2011 May 4;30(9):1804-17. (PMID: 21448132)
J Mol Biol. 2006 May 12;358(4):1023-31. (PMID: 16580682)
Nat Commun. 2016 Dec 20;7:13521. (PMID: 27995908)
Science. 2016 Dec 16;354(6318):1431-1433. (PMID: 27980209)
Nat Struct Mol Biol. 2014 Dec;21(12):1042-6. (PMID: 25362488)
Curr Opin Struct Biol. 2012 Dec;22(6):759-67. (PMID: 22884264)
Mol Cell. 2021 Jan 21;81(2):304-322.e16. (PMID: 33357414)
J Biochem. 2002 Dec;132(6):983-9. (PMID: 12473202)
Elife. 2016 May 09;5:. (PMID: 27159452)
Nat Struct Mol Biol. 2019 Jan;26(1):35-39. (PMID: 30559462)
Nature. 2014 Feb 6;506(7486):107-10. (PMID: 24499919)
Nat Struct Mol Biol. 2016 Jan;23(1):37-44. (PMID: 26619264)
Oncogene. 2004 May 27;23(25):4454-65. (PMID: 15064750)
Nat Microbiol. 2018 Oct;3(10):1115-1121. (PMID: 30177741)
EMBO J. 2017 Jul 14;36(14):2061-2072. (PMID: 28468753)
Cell. 2014 Jun 19;157(7):1632-43. (PMID: 24930395)
Nature. 2012 Feb 22;482(7386):501-6. (PMID: 22358840)
Cell. 2016 Jan 14;164(1-2):91-102. (PMID: 26709046)
Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):213-21. (PMID: 20124702)
FEBS Lett. 2007 Sep 18;581(23):4450-4. (PMID: 17765895)
EMBO J. 2014 Feb 3;33(3):265-76. (PMID: 24424461)
PLoS Biol. 2018 Sep 12;16(9):e2005903. (PMID: 30208026)
Nucleic Acids Res. 2014 Jul;42(Web Server issue):W252-8. (PMID: 24782522)
Nat Struct Mol Biol. 2016 Jan;23(1):7-15. (PMID: 26733220)
Annu Rev Genet. 2018 Nov 23;52:321-348. (PMID: 30476446)
Nat Commun. 2020 Feb 7;11(1):776. (PMID: 32034140)
Mol Cell. 2007 Sep 7;27(5):767-79. (PMID: 17803941)
Elife. 2018 Oct 24;7:. (PMID: 30355441)
RNA. 2011 May;17(5):835-42. (PMID: 21460238)
Nucleic Acids Res. 2008 Nov;36(19):6187-98. (PMID: 18824477)
Nature. 2013 May 2;497(7447):80-5. (PMID: 23636399)
Proc Natl Acad Sci U S A. 2011 Dec 20;108(51):E1392-8. (PMID: 22143755)
Arch Biochem Biophys. 1980 May;201(2):518-26. (PMID: 6901609)
Science. 2016 Jan 1;351(6268):88-91. (PMID: 26721998)
J Biochem. 2018 Mar 1;163(3):177-185. (PMID: 29069440)
Genes Cells. 2005 Dec;10(12):1103-12. (PMID: 16324148)
Nat Struct Mol Biol. 2011 Jun;18(6):715-20. (PMID: 21623367)
Nat Methods. 2017 Apr;14(4):331-332. (PMID: 28250466)
Cell Cycle. 2011 Aug 15;10(16):2691-702. (PMID: 21768774)
Acta Crystallogr D Biol Crystallogr. 2015 Jan 1;71(Pt 1):136-53. (PMID: 25615868)
Nature. 2015 Aug 27;524(7566):493-496. (PMID: 26245381)
Cell. 2014 Jul 3;158(1):121-31. (PMID: 24995983)
Cell. 2016 Nov 17;167(5):1229-1240.e15. (PMID: 27863242)
RNA. 2010 Jun;16(6):1196-204. (PMID: 20427512)
Protein Sci. 2018 Jan;27(1):14-25. (PMID: 28710774)
Biochem Biophys Res Commun. 2013 Jan 11;430(2):745-50. (PMID: 23206692)
Nat Struct Mol Biol. 2019 Apr;26(4):275-280. (PMID: 30911188)
Science. 2009 Dec 4;326(5958):1369-73. (PMID: 19933108)
Cell. 1989 Jun 16;57(6):947-54. (PMID: 2661015)
Substance Nomenclature:: 0 (Adaptor Proteins, Signal Transducing)
0 (Ccdc124 protein, human)
0 (Cell Cycle Proteins)
0 (Intracellular Signaling Peptides and Proteins)
0 (LSO2 protein, S cerevisiae)
0 (PA2G4 protein, human)
0 (Peptides)
0 (RNA, Messenger)
0 (RNA-Binding Proteins)
0 (Ribosomal Proteins)
0 (Saccharomyces cerevisiae Proteins)
9014-25-9 (RNA, Transfer)
Entry Date(s):: Date Created: 20200721 Date Completed: 20200824 Latest Revision: 20240329
Update Code:: 20240329
PubMed Central ID:: PMC7392345
DOI:: 10.1371/journal.pbio.3000780
PMID:: 32687489
: Czasopismo naukowe

Pełny tekst

Cells adjust to nutrient deprivation by reversible translational shutdown. This is accompanied by maintaining inactive ribosomes in a hibernation state, in which they are bound by proteins with inhibitory and protective functions. In eukaryotes, such a function was attributed to suppressor of target of Myb protein 1 (Stm1; SERPINE1 mRNA-binding protein 1 [SERBP1] in mammals), and recently, late-annotated short open reading frame 2 (Lso2; coiled-coil domain containing short open reading frame 124 [CCDC124] in mammals) was found to be involved in translational recovery after starvation from stationary phase. Here, we present cryo-electron microscopy (cryo-EM) structures of translationally inactive yeast and human ribosomes. We found Lso2/CCDC124 accumulating on idle ribosomes in the nonrotated state, in contrast to Stm1/SERBP1-bound ribosomes, which display a rotated state. Lso2/CCDC124 bridges the decoding sites of the small with the GTPase activating center (GAC) of the large subunit. This position allows accommodation of the duplication of multilocus region 34 protein (Dom34)-dependent ribosome recycling system, which splits Lso2-containing, but not Stm1-containing, ribosomes. We propose a model in which Lso2 facilitates rapid translation reactivation by stabilizing the recycling-competent state of inactive ribosomes.
Competing Interests: The authors have declared that no competing interests exist.

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