Ubiquitin in Motion: Structural Studies of the Ubiquitin-Conjugating Enzyme∼Ubiquitin Conjugate
Ubiquitination of proteins provides a powerful and versatile post-translational signal in the eukaryotic cell. The formation of a thioester bond between ubiquitin (Ub) and the active site of a ubiquitin-conjugating enzyme (E2) is critical for the transfer of Ub to substrates. Assembly of a functiona...
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Published in | Biochemistry (Easton) Vol. 50; no. 10; pp. 1624 - 1633 |
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Main Authors | , , , , |
Format | Journal Article |
Language | English |
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United States
American Chemical Society
15.03.2011
American Chemical Society (ACS) |
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Abstract | Ubiquitination of proteins provides a powerful and versatile post-translational signal in the eukaryotic cell. The formation of a thioester bond between ubiquitin (Ub) and the active site of a ubiquitin-conjugating enzyme (E2) is critical for the transfer of Ub to substrates. Assembly of a functional ubiquitin ligase (E3) complex poised for Ub transfer involves recognition and binding of an E2∼Ub conjugate. Therefore, full characterization of the structure and dynamics of E2∼Ub conjugates is required for further mechanistic understanding of Ub transfer reactions. Here we present characterization of the dynamic behavior of E2∼Ub conjugates of two human enzymes, UbcH5c∼Ub and Ubc13∼Ub, in solution as determined by nuclear magnetic resonance and small-angle X-ray scattering. Within each conjugate, Ub retains great flexibility with respect to the E2, indicative of highly dynamic species that adopt manifold orientations. The population distribution of Ub conformations is dictated by the identity of the E2: the UbcH5c∼Ub conjugate populates an array of extended conformations, and the population of Ubc13∼Ub conjugates favors a closed conformation in which the hydrophobic surface of Ub faces helix 2 of Ubc13. We propose that the varied conformations adopted by Ub represent available binding modes of the E2∼Ub species and thus provide insight into the diverse E2∼Ub protein interactome, particularly with regard to interaction with Ub ligases. |
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AbstractList | Ubiquitination of proteins provides a powerful and versatile post-translational signal in the eukaryotic cell. The formation of a thioester bond between ubiquitin (Ub) and the active site of a ubiquitin-conjugating enzyme (E2) is critical for the transfer of Ub to substrates. Assembly of a functional ubiquitin ligase (E3) complex poised for Ub transfer involves recognition and binding of an E2~Ub conjugate. Therefore, full characterization of the structure and dynamics of E2~Ub conjugates is required for further mechanistic understanding of Ub transfer reactions. Here we present characterization of the dynamic behavior of E2~Ub conjugates of two human enzymes, UbcH5c~Ub and Ubc13~Ub, in solution as determined by nuclear magnetic resonance and small-angle X-ray scattering. Within each conjugate, Ub retains great flexibility with respect to the E2, indicative of highly dynamic species that adopt manifold orientations. The population distribution of Ub conformations is dictated by the identity of the E2: the UbcH5c~Ub conjugate populates an array of extended conformations, and the population of Ubc13~Ub conjugates favors a closed conformation in which the hydrophobic surface of Ub faces helix 2 of Ubc13. Finally, we propose that the varied conformations adopted by Ub represent available binding modes of the E2~Ub species and thus provide insight into the diverse E2~Ub protein interactome, particularly with regard to interaction with Ub ligases. Ubiquitination of proteins provides a powerful and versatile post-translational signal in the eukaryotic cell. The formation of a thioester bond between ubiquitin (Ub) and the active site of a ubiquitin-conjugating enzyme (E2) is critical for the transfer of Ub to substrates. Assembly of a functional ubiquitin ligase (E3) complex poised for Ub transfer involves recognition and binding of an E2∼Ub conjugate. Therefore, full characterization of the structure and dynamics of E2∼Ub conjugates is required for further mechanistic understanding of Ub transfer reactions. Here we present characterization of the dynamic behavior of E2∼Ub conjugates of two human enzymes, UbcH5c∼Ub and Ubc13∼Ub, in solution as determined by nuclear magnetic resonance and small-angle X-ray scattering. Within each conjugate, Ub retains great flexibility with respect to the E2, indicative of highly dynamic species that adopt manifold orientations. The population distribution of Ub conformations is dictated by the identity of the E2: the UbcH5c∼Ub conjugate populates an array of extended conformations, and the population of Ubc13∼Ub conjugates favors a closed conformation in which the hydrophobic surface of Ub faces helix 2 of Ubc13. We propose that the varied conformations adopted by Ub represent available binding modes of the E2∼Ub species and thus provide insight into the diverse E2∼Ub protein interactome, particularly with regard to interaction with Ub ligases. |
Author | Pruneda, Jonathan N Klevit, Rachel E Bolton, Laura J Stoll, Kate E Brzovic, Peter S |
Author_xml | – sequence: 1 givenname: Jonathan N surname: Pruneda fullname: Pruneda, Jonathan N – sequence: 2 givenname: Kate E surname: Stoll fullname: Stoll, Kate E – sequence: 3 givenname: Laura J surname: Bolton fullname: Bolton, Laura J – sequence: 4 givenname: Peter S surname: Brzovic fullname: Brzovic, Peter S – sequence: 5 givenname: Rachel E surname: Klevit fullname: Klevit, Rachel E email: klevit@uw.edu |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/21226485$$D View this record in MEDLINE/PubMed https://www.osti.gov/biblio/1028547$$D View this record in Osti.gov |
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Cites_doi | 10.1073/pnas.0914821107 10.1083/jcb.200406001 10.1007/s00239-009-9225-6 10.1146/annurev.biochem.70.1.503 10.1073/pnas.0504466102 10.1016/j.molcel.2009.11.010 10.1016/j.jmb.2008.10.044 10.1074/jbc.M212353200 10.1073/pnas.0509418102 10.1021/ja069124n 10.1016/S0969-2126(01)00657-8 10.1007/BF00197809 10.1016/j.str.2009.11.007 10.1007/BF00404272 10.1016/S0021-9258(18)34024-9 10.1038/90373 10.1074/jbc.M211240200 10.1073/pnas.0836054100 10.1038/nsmb1148 10.1016/j.molcel.2006.02.008 10.1107/S0021889895007047 10.1107/S0021889892001663 10.1006/jmbi.1999.2859 10.1038/nrm2780 10.1107/S0021889803012779 10.1021/bi901686j |
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References | 16365295 - Proc Natl Acad Sci U S A. 2005 Dec 27;102(52):18890-5 19851334 - Nat Rev Mol Cell Biol. 2009 Nov;10(11):755-64 11395416 - Annu Rev Biochem. 2001;70:503-33 15545318 - J Cell Biol. 2004 Nov 22;167(4):649-59 22911360 - J Biomol NMR. 1994 Sep;4(5):603-14 19928833 - Biochemistry. 2009 Dec 29;48(51):12169-79 12732733 - Proc Natl Acad Sci U S A. 2003 May 13;100(10):5646-51 16162672 - Proc Natl Acad Sci U S A. 2005 Sep 27;102(39):14046-51 12569095 - J Biol Chem. 2003 Apr 11;278(15):13151-8 16543155 - Mol Cell. 2006 Mar 17;21(6):873-80 20064473 - Mol Cell. 2009 Dec 25;36(6):1095-102 17411046 - J Am Chem Soc. 2007 May 2;129(17):5656-64 19452197 - J Mol Evol. 2009 Jun;68(6):616-28 11473255 - Nat Struct Biol. 2001 Aug;8(8):669-73 20152160 - Structure. 2010 Jan 13;18(1):138-47 6286650 - J Biol Chem. 1982 Sep 10;257(17):10329-37 10388568 - J Mol Biol. 1999 Jul 2;290(1):213-28 12524449 - J Biol Chem. 2003 Mar 14;278(11):9448-57 18996392 - J Mol Biol. 2009 Jan 16;385(2):507-19 20133640 - Proc Natl Acad Sci U S A. 2010 Feb 16;107(7):2848-53 16980971 - Nat Struct Mol Biol. 2006 Oct;13(10):915-20 11591345 - Structure. 2001 Oct;9(10):897-904 8520220 - J Biomol NMR. 1995 Nov;6(3):277-93 Michelle C. (ref12/cit12) 2009; 68 Svergun D. I. (ref19/cit19) 1992; 25 Plafker S. M. (ref26/cit26) 2004; 167 Brzovic P. S. (ref15/cit15) 2006; 21 Miura T. (ref22/cit22) 1999; 290 Huang A. (ref9/cit9) 2009; 385 McKenna S. (ref24/cit24) 2003; 278 Ye Y. (ref2/cit2) 2009; 10 Serniwka S. A. (ref5/cit5) 2009; 48 Haas A. L. (ref11/cit11) 1982; 257 Kim D. W. (ref25/cit25) 2005; 102 Bernadó P. (ref21/cit21) 2007; 129 Eddins M. J. (ref3/cit3) 2006; 13 Brzovic P. S. (ref14/cit14) 2003; 100 Siepmann T. J. (ref10/cit10) 2003; 278 Levin I. (ref23/cit23) 2010; 107 Ozkan E. (ref8/cit8) 2005; 102 Johnson B. A. (ref17/cit17) 1994; 4 Hamilton K. S. (ref4/cit4) 2001; 9 Kamadurai H. B. (ref7/cit7) 2009; 36 Moraes T. F. (ref13/cit13) 2001; 8 Sakata E. (ref6/cit6) 2010; 18 Pickart C. M. (ref1/cit1) 2001; 70 Svergun D. (ref20/cit20) 1995; 28 Delaglio F. (ref16/cit16) 1995; 6 Konarev P. V. (ref18/cit18) 2003; 36 |
References_xml | – volume: 107 start-page: 2848 year: 2010 ident: ref23/cit23 publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.0914821107 contributor: fullname: Levin I. – volume: 167 start-page: 649 year: 2004 ident: ref26/cit26 publication-title: J. Cell Biol. doi: 10.1083/jcb.200406001 contributor: fullname: Plafker S. M. – volume: 68 start-page: 616 year: 2009 ident: ref12/cit12 publication-title: J. Mol. Evol. doi: 10.1007/s00239-009-9225-6 contributor: fullname: Michelle C. – volume: 70 start-page: 503 year: 2001 ident: ref1/cit1 publication-title: Annu. Rev. Biochem. doi: 10.1146/annurev.biochem.70.1.503 contributor: fullname: Pickart C. M. – volume: 102 start-page: 14046 year: 2005 ident: ref25/cit25 publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.0504466102 contributor: fullname: Kim D. W. – volume: 36 start-page: 1095 year: 2009 ident: ref7/cit7 publication-title: Mol. Cell doi: 10.1016/j.molcel.2009.11.010 contributor: fullname: Kamadurai H. B. – volume: 385 start-page: 507 year: 2009 ident: ref9/cit9 publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2008.10.044 contributor: fullname: Huang A. – volume: 278 start-page: 13151 year: 2003 ident: ref24/cit24 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M212353200 contributor: fullname: McKenna S. – volume: 102 start-page: 18890 year: 2005 ident: ref8/cit8 publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.0509418102 contributor: fullname: Ozkan E. – volume: 129 start-page: 5656 year: 2007 ident: ref21/cit21 publication-title: J. Am. Chem. Soc. doi: 10.1021/ja069124n contributor: fullname: Bernadó P. – volume: 9 start-page: 897 year: 2001 ident: ref4/cit4 publication-title: Structure doi: 10.1016/S0969-2126(01)00657-8 contributor: fullname: Hamilton K. S. – volume: 6 start-page: 277 year: 1995 ident: ref16/cit16 publication-title: J. Biomol. NMR doi: 10.1007/BF00197809 contributor: fullname: Delaglio F. – volume: 18 start-page: 138 year: 2010 ident: ref6/cit6 publication-title: Structure doi: 10.1016/j.str.2009.11.007 contributor: fullname: Sakata E. – volume: 4 start-page: 603 year: 1994 ident: ref17/cit17 publication-title: J. Biomol. NMR doi: 10.1007/BF00404272 contributor: fullname: Johnson B. A. – volume: 257 start-page: 10329 year: 1982 ident: ref11/cit11 publication-title: J. Biol. Chem. doi: 10.1016/S0021-9258(18)34024-9 contributor: fullname: Haas A. L. – volume: 8 start-page: 669 year: 2001 ident: ref13/cit13 publication-title: Nat. Struct. Mol. Biol. doi: 10.1038/90373 contributor: fullname: Moraes T. F. – volume: 278 start-page: 9448 year: 2003 ident: ref10/cit10 publication-title: J. Biol. Chem. doi: 10.1074/jbc.M211240200 contributor: fullname: Siepmann T. J. – volume: 100 start-page: 5646 year: 2003 ident: ref14/cit14 publication-title: Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.0836054100 contributor: fullname: Brzovic P. S. – volume: 13 start-page: 915 year: 2006 ident: ref3/cit3 publication-title: Nat. Struct. Mol. Biol. doi: 10.1038/nsmb1148 contributor: fullname: Eddins M. J. – volume: 21 start-page: 873 year: 2006 ident: ref15/cit15 publication-title: Mol. Cell doi: 10.1016/j.molcel.2006.02.008 contributor: fullname: Brzovic P. S. – volume: 28 start-page: 768 year: 1995 ident: ref20/cit20 publication-title: J. Appl. Crystallogr. doi: 10.1107/S0021889895007047 contributor: fullname: Svergun D. – volume: 25 start-page: 495 year: 1992 ident: ref19/cit19 publication-title: J. Appl. Crystallogr. doi: 10.1107/S0021889892001663 contributor: fullname: Svergun D. I. – volume: 290 start-page: 213 year: 1999 ident: ref22/cit22 publication-title: J. Mol. Biol. doi: 10.1006/jmbi.1999.2859 contributor: fullname: Miura T. – volume: 10 start-page: 755 year: 2009 ident: ref2/cit2 publication-title: Nat. Rev. Mol. Cell Biol. doi: 10.1038/nrm2780 contributor: fullname: Ye Y. – volume: 36 start-page: 1277 year: 2003 ident: ref18/cit18 publication-title: J. Appl. Crystallogr. doi: 10.1107/S0021889803012779 contributor: fullname: Konarev P. V. – volume: 48 start-page: 12169 year: 2009 ident: ref5/cit5 publication-title: Biochemistry doi: 10.1021/bi901686j contributor: fullname: Serniwka S. A. |
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Snippet | Ubiquitination of proteins provides a powerful and versatile post-translational signal in the eukaryotic cell. The formation of a thioester bond between... |
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SubjectTerms | 60 APPLIED LIFE SCIENCES BASIC BIOLOGICAL SCIENCES Crystallography, X-Ray DISTRIBUTION Environmental Molecular Sciences Laboratory ENZYMES FLEXIBILITY FUNCTIONALS Humans LIGASES Models, Molecular NUCLEAR MAGNETIC RESONANCE Nuclear Magnetic Resonance, Biomolecular Protein Binding Protein Structure, Quaternary PROTEINS SCATTERING SUBSTRATES TRANSFER REACTIONS Ubiquitin - chemistry Ubiquitin - metabolism Ubiquitin-Conjugating Enzymes - chemistry Ubiquitin-Conjugating Enzymes - metabolism |
Title | Ubiquitin in Motion: Structural Studies of the Ubiquitin-Conjugating Enzyme∼Ubiquitin Conjugate |
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