The Active Form of E6-associated protein (E6AP)/UBE3A Ubiquitin Ligase Is an Oligomer
Employing 125I-polyubiquitin chain formation as a functional readout of ligase activity, biochemical and biophysical evidence demonstrates that catalytically active E6-associated protein (E6AP)/UBE3A is an oligomer. Based on an extant structure previously discounted as an artifact of crystal packing...
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Published in | The Journal of biological chemistry Vol. 289; no. 2; pp. 1033 - 1048 |
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Main Authors | , , , |
Format | Journal Article |
Language | English |
Published |
United States
Elsevier Inc
10.01.2014
American Society for Biochemistry and Molecular Biology |
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Abstract | Employing 125I-polyubiquitin chain formation as a functional readout of ligase activity, biochemical and biophysical evidence demonstrates that catalytically active E6-associated protein (E6AP)/UBE3A is an oligomer. Based on an extant structure previously discounted as an artifact of crystal packing forces, we propose that the fully active form of E6AP is a trimer, analysis of which reveals a buried surface of 7508 Å2 and radially symmetric interacting residues that are conserved within the Hect (homologous to E6AP C terminus) ligase superfamily. An absolutely conserved interaction between Phe727 and a hydrophobic pocket present on the adjacent subunit is critical for trimer stabilization because mutation disrupts the oligomer and decreases kcat 62-fold but fails to affect E2∼ubiquitin binding or subsequent formation of the Hect domain Cys820∼ubiquitin thioester catalytic intermediate. Exogenous N-acetylphenylalanylamide reversibly antagonizes Phe727-dependent trimer formation and catalytic activity (Ki = 12 mm), as does a conserved α-helical peptide corresponding to residues 474–490 of E6AP isoform 1 (Ki = 22 μm) reported to bind the hydrophobic pocket of other Hect ligases, presumably blocking Phe727 intercalation and trimer formation. Conversely, oncogenic human papillomavirus-16/18 E6 protein significantly enhances E6AP catalytic activity by promoting trimer formation (Kactivation = 1.5 nm) through the ability of E6 to form homodimers. Recombinant E6 protein additionally rescues the kcat defect of the Phe727 mutation and that of a specific loss-of-function Angelman syndrome mutation that promotes trimer destabilization. The present findings codify otherwise disparate observations regarding the mechanism of E6AP and related Hect ligases in addition to suggesting therapeutic approaches for modulating ligase activity.
E6AP/UBE3A is a Hect ligase implicated in neurodevelopment and cell transformation.
Kinetic/biophysical analyses demonstrate that E6AP oligomerization is required for polyubiquitin degradation signal assembly and that changes in oligomerization regulates such activity.
E6AP oligomerization accounts for opposing effects of mutation and HPV16/18 E6 protein.
These findings explain in part the etiology of specific Angelman syndrome mutations and E6-mediated cell transformation. |
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AbstractList | Employing 125I-polyubiquitin chain formation as a functional readout of ligase activity, biochemical and biophysical evidence demonstrates that catalytically active E6-associated protein (E6AP)/UBE3A is an oligomer. Based on an extant structure previously discounted as an artifact of crystal packing forces, we propose that the fully active form of E6AP is a trimer, analysis of which reveals a buried surface of 7508Å2 and radially symmetric interacting residues that are conserved within the Hect (homologous to E6AP C terminus) ligase superfamily. An absolutely conserved interaction between Phe(727) and a hydrophobic pocket present on the adjacent subunit is critical for trimer stabilization because mutation disrupts the oligomer and decreases kcat 62-fold but fails to affect E2 ubiquitin binding or subsequent formation of the Hect domain Cys(820) ubiquitin thioester catalytic intermediate. Exogenous N-acetylphenylalanylamide reversibly antagonizes Phe(727)-dependent trimer formation and catalytic activity (Ki12 mM), as does a conserved-helical peptide corresponding to residues 474–490 of E6A Pisoform 1 (Ki22M) reported to bind the hydrophobic pocket of other Hect ligases, presumably blocking Phe(727) intercalation and trimer formation. Conversely, oncogenic human papillomavirus-16/18 E6 protein significantly enhances E6AP catalytic activity by promoting trimer formation (Kactivation 1.5 nM) through the ability of E6 to form homodimers. Recombinant E6 protein additionally rescues the kcat defect of the Phe(727) mutation and that of a specific loss-of-function Angelman syndrome mutation that promotes trimer destabilization. The present findings codify otherwise disparate observations regarding the mechanism of E6AP and related Hect ligases in addition to suggesting therapeutic approaches for modulating ligase activity. Employing 125I-polyubiquitin chain formation as a functional readout of ligase activity, biochemical and biophysical evidence demonstrates that catalytically active E6-associated protein (E6AP)/UBE3A is an oligomer. Based on an extant structure previously discounted as an artifact of crystal packing forces, we propose that the fully active form of E6AP is a trimer, analysis of which reveals a buried surface of 7508 Å2 and radially symmetric interacting residues that are conserved within the Hect (homologous to E6AP C terminus) ligase superfamily. An absolutely conserved interaction between Phe727 and a hydrophobic pocket present on the adjacent subunit is critical for trimer stabilization because mutation disrupts the oligomer and decreases kcat 62-fold but fails to affect E2∼ubiquitin binding or subsequent formation of the Hect domain Cys820∼ubiquitin thioester catalytic intermediate. Exogenous N-acetylphenylalanylamide reversibly antagonizes Phe727-dependent trimer formation and catalytic activity (Ki = 12 mm), as does a conserved α-helical peptide corresponding to residues 474–490 of E6AP isoform 1 (Ki = 22 μm) reported to bind the hydrophobic pocket of other Hect ligases, presumably blocking Phe727 intercalation and trimer formation. Conversely, oncogenic human papillomavirus-16/18 E6 protein significantly enhances E6AP catalytic activity by promoting trimer formation (Kactivation = 1.5 nm) through the ability of E6 to form homodimers. Recombinant E6 protein additionally rescues the kcat defect of the Phe727 mutation and that of a specific loss-of-function Angelman syndrome mutation that promotes trimer destabilization. The present findings codify otherwise disparate observations regarding the mechanism of E6AP and related Hect ligases in addition to suggesting therapeutic approaches for modulating ligase activity. E6AP/UBE3A is a Hect ligase implicated in neurodevelopment and cell transformation. Kinetic/biophysical analyses demonstrate that E6AP oligomerization is required for polyubiquitin degradation signal assembly and that changes in oligomerization regulates such activity. E6AP oligomerization accounts for opposing effects of mutation and HPV16/18 E6 protein. These findings explain in part the etiology of specific Angelman syndrome mutations and E6-mediated cell transformation. Background: E6AP/UBE3A is a Hect ligase implicated in neurodevelopment and cell transformation. Results: Kinetic/biophysical analyses demonstrate that E6AP oligomerization is required for polyubiquitin degradation signal assembly and that changes in oligomerization regulates such activity. Conclusion: E6AP oligomerization accounts for opposing effects of mutation and HPV16/18 E6 protein. Significance: These findings explain in part the etiology of specific Angelman syndrome mutations and E6-mediated cell transformation. Employing 125 I-polyubiquitin chain formation as a functional readout of ligase activity, biochemical and biophysical evidence demonstrates that catalytically active E6-associated protein (E6AP)/UBE3A is an oligomer. Based on an extant structure previously discounted as an artifact of crystal packing forces, we propose that the fully active form of E6AP is a trimer, analysis of which reveals a buried surface of 7508 Å 2 and radially symmetric interacting residues that are conserved within the Hect (homologous to E6AP C terminus) ligase superfamily. An absolutely conserved interaction between Phe 727 and a hydrophobic pocket present on the adjacent subunit is critical for trimer stabilization because mutation disrupts the oligomer and decreases k cat 62-fold but fails to affect E2∼ubiquitin binding or subsequent formation of the Hect domain Cys 820 ∼ubiquitin thioester catalytic intermediate. Exogenous N -acetylphenylalanylamide reversibly antagonizes Phe 727 -dependent trimer formation and catalytic activity ( K i = 12 m m ), as does a conserved α-helical peptide corresponding to residues 474–490 of E6AP isoform 1 ( K i = 22 μ m ) reported to bind the hydrophobic pocket of other Hect ligases, presumably blocking Phe 727 intercalation and trimer formation. Conversely, oncogenic human papillomavirus-16/18 E6 protein significantly enhances E6AP catalytic activity by promoting trimer formation ( K activation = 1.5 n m ) through the ability of E6 to form homodimers. Recombinant E6 protein additionally rescues the k cat defect of the Phe 727 mutation and that of a specific loss-of-function Angelman syndrome mutation that promotes trimer destabilization. The present findings codify otherwise disparate observations regarding the mechanism of E6AP and related Hect ligases in addition to suggesting therapeutic approaches for modulating ligase activity. |
Author | Klein, Jennifer M. Edwards, Daniel J. Haas, Arthur L. Ronchi, Virginia P. |
Author_xml | – sequence: 1 givenname: Virginia P. surname: Ronchi fullname: Ronchi, Virginia P. organization: Department of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center, New Orleans, Louisiana 70112 – sequence: 2 givenname: Jennifer M. surname: Klein fullname: Klein, Jennifer M. organization: Department of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center, New Orleans, Louisiana 70112 – sequence: 3 givenname: Daniel J. surname: Edwards fullname: Edwards, Daniel J. organization: Department of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center, New Orleans, Louisiana 70112 – sequence: 4 givenname: Arthur L. surname: Haas fullname: Haas, Arthur L. email: ahaas@lsuhsc.edu organization: Department of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center, New Orleans, Louisiana 70112 |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/24273172$$D View this record in MEDLINE/PubMed |
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Copyright | 2014 © 2014 ASBMB. Currently published by Elsevier Inc; originally published by American Society for Biochemistry and Molecular Biology. 2014 by The American Society for Biochemistry and Molecular Biology, Inc. 2014 |
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Keywords | Enzyme Mechanisms Ubiquitin E3 Ubiquitin Ligase Hect Ligase Enzyme Kinetics Kinetics |
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Snippet | Employing 125I-polyubiquitin chain formation as a functional readout of ligase activity, biochemical and biophysical evidence demonstrates that catalytically... Background: E6AP/UBE3A is a Hect ligase implicated in neurodevelopment and cell transformation. Results: Kinetic/biophysical analyses demonstrate that E6AP... |
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SubjectTerms | Amino Acid Sequence Angelman Syndrome - genetics Angelman Syndrome - metabolism Animals Binding Sites - genetics Biocatalysis E3 Ubiquitin Ligase Electrophoresis, Polyacrylamide Gel Enzyme Kinetics Enzyme Mechanisms Enzymology Hect Ligase Humans Hydrogen Bonding Iodine Radioisotopes Isoenzymes - chemistry Isoenzymes - genetics Isoenzymes - metabolism Kinetics Models, Molecular Molecular Sequence Data Mutation Phylogeny Polyubiquitin - metabolism Protein Multimerization Protein Structure, Secondary Protein Structure, Tertiary Sequence Homology, Amino Acid Sf9 Cells Ubiquitin Ubiquitin - metabolism Ubiquitin-Protein Ligases - chemistry Ubiquitin-Protein Ligases - genetics Ubiquitin-Protein Ligases - metabolism |
Title | The Active Form of E6-associated protein (E6AP)/UBE3A Ubiquitin Ligase Is an Oligomer |
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