SUMO modification of the ubiquitin-conjugating enzyme E2-25K

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Standard

SUMO modification of the ubiquitin-conjugating enzyme E2-25K. / Pichler, Andrea; Knipscheer, Puck; Oberhofer, Edith; van Dijk, Willem J; Körner, Roman; Olsen, Jesper Velgaard; Jentsch, Stefan; Melchior, Frauke; Sixma, Titia K.

In: Nature Structural and Molecular Biology, Vol. 12, No. 3, 2005, p. 264-9.

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

Harvard

Pichler, A, Knipscheer, P, Oberhofer, E, van Dijk, WJ, Körner, R, Olsen, JV, Jentsch, S, Melchior, F & Sixma, TK 2005, 'SUMO modification of the ubiquitin-conjugating enzyme E2-25K', Nature Structural and Molecular Biology, vol. 12, no. 3, pp. 264-9. https://doi.org/10.1038/nsmb903

APA

Pichler, A., Knipscheer, P., Oberhofer, E., van Dijk, W. J., Körner, R., Olsen, J. V., Jentsch, S., Melchior, F., & Sixma, T. K. (2005). SUMO modification of the ubiquitin-conjugating enzyme E2-25K. Nature Structural and Molecular Biology, 12(3), 264-9. https://doi.org/10.1038/nsmb903

Vancouver

Pichler A, Knipscheer P, Oberhofer E, van Dijk WJ, Körner R, Olsen JV et al. SUMO modification of the ubiquitin-conjugating enzyme E2-25K. Nature Structural and Molecular Biology. 2005;12(3):264-9. https://doi.org/10.1038/nsmb903

Author

Pichler, Andrea ; Knipscheer, Puck ; Oberhofer, Edith ; van Dijk, Willem J ; Körner, Roman ; Olsen, Jesper Velgaard ; Jentsch, Stefan ; Melchior, Frauke ; Sixma, Titia K. / SUMO modification of the ubiquitin-conjugating enzyme E2-25K. In: Nature Structural and Molecular Biology. 2005 ; Vol. 12, No. 3. pp. 264-9.

Bibtex

@article{62e8ec90457011df928f000ea68e967b,
title = "SUMO modification of the ubiquitin-conjugating enzyme E2-25K",
abstract = "Post-translational modification with small ubiquitin-related modifier (SUMO) alters the function of many proteins, but the molecular mechanisms and consequences of this modification are still poorly defined. During a screen for novel SUMO1 targets, we identified the ubiquitin-conjugating enzyme E2-25K (Hip2). SUMO attachment severely impairs E2-25K ubiquitin thioester and unanchored ubiquitin chain formation in vitro. Crystal structures of E2-25K(1-155) and of the E2-25K(1-155)-SUMO conjugate (E2-25K(*)SUMO) indicate that SUMO attachment interferes with E1 interaction through its location on the N-terminal helix. The SUMO acceptor site in E2-25K, Lys14, does not conform to the consensus site found in most SUMO targets (PsiKXE), and functions only in the context of an alpha-helix. In contrast, adjacent SUMO consensus sites are modified only when in unstructured peptides. The demonstration that secondary structure elements are part of SUMO attachment signals could contribute to a better prediction of SUMO targets.",
author = "Andrea Pichler and Puck Knipscheer and Edith Oberhofer and {van Dijk}, {Willem J} and Roman K{\"o}rner and Olsen, {Jesper Velgaard} and Stefan Jentsch and Frauke Melchior and Sixma, {Titia K}",
note = "Keywords: Amino Acid Sequence; Consensus Sequence; Crystallization; Hela Cells; Humans; Molecular Sequence Data; Protein Interaction Mapping; Protein Processing, Post-Translational; Protein Structure, Secondary; SUMO-1 Protein; Ubiquitin-Conjugating Enzymes",
year = "2005",
doi = "10.1038/nsmb903",
language = "English",
volume = "12",
pages = "264--9",
journal = "Nature Structural and Molecular Biology",
issn = "1545-9993",
publisher = "nature publishing group",
number = "3",

}

RIS

TY - JOUR

T1 - SUMO modification of the ubiquitin-conjugating enzyme E2-25K

AU - Pichler, Andrea

AU - Knipscheer, Puck

AU - Oberhofer, Edith

AU - van Dijk, Willem J

AU - Körner, Roman

AU - Olsen, Jesper Velgaard

AU - Jentsch, Stefan

AU - Melchior, Frauke

AU - Sixma, Titia K

N1 - Keywords: Amino Acid Sequence; Consensus Sequence; Crystallization; Hela Cells; Humans; Molecular Sequence Data; Protein Interaction Mapping; Protein Processing, Post-Translational; Protein Structure, Secondary; SUMO-1 Protein; Ubiquitin-Conjugating Enzymes

PY - 2005

Y1 - 2005

N2 - Post-translational modification with small ubiquitin-related modifier (SUMO) alters the function of many proteins, but the molecular mechanisms and consequences of this modification are still poorly defined. During a screen for novel SUMO1 targets, we identified the ubiquitin-conjugating enzyme E2-25K (Hip2). SUMO attachment severely impairs E2-25K ubiquitin thioester and unanchored ubiquitin chain formation in vitro. Crystal structures of E2-25K(1-155) and of the E2-25K(1-155)-SUMO conjugate (E2-25K(*)SUMO) indicate that SUMO attachment interferes with E1 interaction through its location on the N-terminal helix. The SUMO acceptor site in E2-25K, Lys14, does not conform to the consensus site found in most SUMO targets (PsiKXE), and functions only in the context of an alpha-helix. In contrast, adjacent SUMO consensus sites are modified only when in unstructured peptides. The demonstration that secondary structure elements are part of SUMO attachment signals could contribute to a better prediction of SUMO targets.

AB - Post-translational modification with small ubiquitin-related modifier (SUMO) alters the function of many proteins, but the molecular mechanisms and consequences of this modification are still poorly defined. During a screen for novel SUMO1 targets, we identified the ubiquitin-conjugating enzyme E2-25K (Hip2). SUMO attachment severely impairs E2-25K ubiquitin thioester and unanchored ubiquitin chain formation in vitro. Crystal structures of E2-25K(1-155) and of the E2-25K(1-155)-SUMO conjugate (E2-25K(*)SUMO) indicate that SUMO attachment interferes with E1 interaction through its location on the N-terminal helix. The SUMO acceptor site in E2-25K, Lys14, does not conform to the consensus site found in most SUMO targets (PsiKXE), and functions only in the context of an alpha-helix. In contrast, adjacent SUMO consensus sites are modified only when in unstructured peptides. The demonstration that secondary structure elements are part of SUMO attachment signals could contribute to a better prediction of SUMO targets.

U2 - 10.1038/nsmb903

DO - 10.1038/nsmb903

M3 - Journal article

C2 - 15723079

VL - 12

SP - 264

EP - 269

JO - Nature Structural and Molecular Biology

JF - Nature Structural and Molecular Biology

SN - 1545-9993

IS - 3

ER -

ID: 19160390