Noncovalent interaction between Ubc9 and SUMO promotes SUMO chain formation

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Noncovalent interaction between Ubc9 and SUMO promotes SUMO chain formation. / Knipscheer, Puck; van Dijk, Willem J; Olsen, Jesper Velgaard; Mann, Matthias; Sixma, Titia K.

In: EMBO Journal, Vol. 26, No. 11, 2007, p. 2797-807.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Knipscheer, P, van Dijk, WJ, Olsen, JV, Mann, M & Sixma, TK 2007, 'Noncovalent interaction between Ubc9 and SUMO promotes SUMO chain formation', EMBO Journal, vol. 26, no. 11, pp. 2797-807. https://doi.org/10.1038/sj.emboj.7601711

APA

Knipscheer, P., van Dijk, W. J., Olsen, J. V., Mann, M., & Sixma, T. K. (2007). Noncovalent interaction between Ubc9 and SUMO promotes SUMO chain formation. EMBO Journal, 26(11), 2797-807. https://doi.org/10.1038/sj.emboj.7601711

Vancouver

Knipscheer P, van Dijk WJ, Olsen JV, Mann M, Sixma TK. Noncovalent interaction between Ubc9 and SUMO promotes SUMO chain formation. EMBO Journal. 2007;26(11):2797-807. https://doi.org/10.1038/sj.emboj.7601711

Author

Knipscheer, Puck ; van Dijk, Willem J ; Olsen, Jesper Velgaard ; Mann, Matthias ; Sixma, Titia K. / Noncovalent interaction between Ubc9 and SUMO promotes SUMO chain formation. In: EMBO Journal. 2007 ; Vol. 26, No. 11. pp. 2797-807.

Bibtex

@article{b2c21e7e1d3e4a5aa90501e2e9702dc5,
title = "Noncovalent interaction between Ubc9 and SUMO promotes SUMO chain formation",
abstract = "The ubiquitin-related modifier SUMO regulates a wide range of cellular processes by post-translational modification with one, or a chain of SUMO molecules. Sumoylation is achieved by the sequential action of several enzymes in which the E2, Ubc9, transfers SUMO from the E1 to the target mostly with the help of an E3 enzyme. In this process, Ubc9 not only forms a thioester bond with SUMO, but also interacts with SUMO noncovalently. Here, we show that this noncovalent interaction promotes the formation of short SUMO chains on targets such as Sp100 and HDAC4. We present a crystal structure of the noncovalent Ubc9-SUMO1 complex, showing that SUMO is located far from the E2 active site and resembles the noncovalent interaction site for ubiquitin on UbcH5c and Mms2. Structural comparison suggests a model for poly-sumoylation involving a mechanism analogous to Mms2-Ubc13-mediated ubiquitin chain formation.",
author = "Puck Knipscheer and {van Dijk}, {Willem J} and Olsen, {Jesper Velgaard} and Matthias Mann and Sixma, {Titia K}",
note = "Keywords: Amino Acid Sequence; Animals; Calorimetry; Chromatography, Gel; Crystallography, X-Ray; Electrophoretic Mobility Shift Assay; Mass Spectrometry; Mice; Models, Molecular; Molecular Sequence Data; SUMO-1 Protein; Ubiquitin-Conjugating Enzymes",
year = "2007",
doi = "10.1038/sj.emboj.7601711",
language = "English",
volume = "26",
pages = "2797--807",
journal = "E M B O Journal",
issn = "0261-4189",
publisher = "Wiley-Blackwell",
number = "11",

}

RIS

TY - JOUR

T1 - Noncovalent interaction between Ubc9 and SUMO promotes SUMO chain formation

AU - Knipscheer, Puck

AU - van Dijk, Willem J

AU - Olsen, Jesper Velgaard

AU - Mann, Matthias

AU - Sixma, Titia K

N1 - Keywords: Amino Acid Sequence; Animals; Calorimetry; Chromatography, Gel; Crystallography, X-Ray; Electrophoretic Mobility Shift Assay; Mass Spectrometry; Mice; Models, Molecular; Molecular Sequence Data; SUMO-1 Protein; Ubiquitin-Conjugating Enzymes

PY - 2007

Y1 - 2007

N2 - The ubiquitin-related modifier SUMO regulates a wide range of cellular processes by post-translational modification with one, or a chain of SUMO molecules. Sumoylation is achieved by the sequential action of several enzymes in which the E2, Ubc9, transfers SUMO from the E1 to the target mostly with the help of an E3 enzyme. In this process, Ubc9 not only forms a thioester bond with SUMO, but also interacts with SUMO noncovalently. Here, we show that this noncovalent interaction promotes the formation of short SUMO chains on targets such as Sp100 and HDAC4. We present a crystal structure of the noncovalent Ubc9-SUMO1 complex, showing that SUMO is located far from the E2 active site and resembles the noncovalent interaction site for ubiquitin on UbcH5c and Mms2. Structural comparison suggests a model for poly-sumoylation involving a mechanism analogous to Mms2-Ubc13-mediated ubiquitin chain formation.

AB - The ubiquitin-related modifier SUMO regulates a wide range of cellular processes by post-translational modification with one, or a chain of SUMO molecules. Sumoylation is achieved by the sequential action of several enzymes in which the E2, Ubc9, transfers SUMO from the E1 to the target mostly with the help of an E3 enzyme. In this process, Ubc9 not only forms a thioester bond with SUMO, but also interacts with SUMO noncovalently. Here, we show that this noncovalent interaction promotes the formation of short SUMO chains on targets such as Sp100 and HDAC4. We present a crystal structure of the noncovalent Ubc9-SUMO1 complex, showing that SUMO is located far from the E2 active site and resembles the noncovalent interaction site for ubiquitin on UbcH5c and Mms2. Structural comparison suggests a model for poly-sumoylation involving a mechanism analogous to Mms2-Ubc13-mediated ubiquitin chain formation.

U2 - 10.1038/sj.emboj.7601711

DO - 10.1038/sj.emboj.7601711

M3 - Journal article

C2 - 17491593

VL - 26

SP - 2797

EP - 2807

JO - E M B O Journal

JF - E M B O Journal

SN - 0261-4189

IS - 11

ER -

ID: 46461442