NMR chemical shift assignments of a complex between SUMO-1 and SIM peptide derived from the C-terminus of Daxx

Mandar T. Naik; Che Chang Chang; Nandita M. Naik; Camy C.H. Kung; Hsiu Ming Shih; Tai Huang Huang

doi:10.1007/s12104-010-9271-4

NMR chemical shift assignments of a complex between SUMO-1 and SIM peptide derived from the C-terminus of Daxx

Mandar T. Naik, Che Chang Chang, Nandita M. Naik, Camy C.H. Kung, Hsiu Ming Shih, Tai Huang Huang^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

3 Citations (Scopus)

Abstract

Small Ubiquitin-like MOdifiers (SUMOs) are ubiquitin-like proteins known to covalently modify large number of cellular proteins. The mammalian SUMO family includes four paralogues, SUMO-1 through SUMO-4. Death-associated protein-6, Daxx, is a 740 residue important transcription corepressor known to represses transcriptional potential of several sumolyted transcription factors. Daxx also plays important role in apoptosis. Both terminals of Daxx harbor separate SUMO Interaction Motifs (SIM), which mediate its interaction with SUMO and hence the sumolyted transcription factors. The C-terminal SIM of Daxx preferentially binds SUMO-1. Practically complete ¹H, ¹³C and ¹⁵N resonance assignments for the complex between SUMO-1 and 20 residue Daxx C-terminal SIM peptide are reported here.

Original language	English
Pages (from-to)	75-77
Number of pages	3
Journal	Biomolecular NMR Assignments
Volume	5
Issue number	1
DOIs	https://doi.org/10.1007/s12104-010-9271-4
Publication status	Published - 2011 Apr
Externally published	Yes

Keywords

Daxx
Promyelocytic leukemia
SUMO
SUMO interaction motif

ASJC Scopus subject areas

Structural Biology
Biochemistry

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10.1007/s12104-010-9271-4

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title = "NMR chemical shift assignments of a complex between SUMO-1 and SIM peptide derived from the C-terminus of Daxx",

abstract = "Small Ubiquitin-like MOdifiers (SUMOs) are ubiquitin-like proteins known to covalently modify large number of cellular proteins. The mammalian SUMO family includes four paralogues, SUMO-1 through SUMO-4. Death-associated protein-6, Daxx, is a 740 residue important transcription corepressor known to represses transcriptional potential of several sumolyted transcription factors. Daxx also plays important role in apoptosis. Both terminals of Daxx harbor separate SUMO Interaction Motifs (SIM), which mediate its interaction with SUMO and hence the sumolyted transcription factors. The C-terminal SIM of Daxx preferentially binds SUMO-1. Practically complete 1H, 13C and 15N resonance assignments for the complex between SUMO-1 and 20 residue Daxx C-terminal SIM peptide are reported here.",

keywords = "Daxx, Promyelocytic leukemia, SUMO, SUMO interaction motif",

author = "Naik, {Mandar T.} and Chang, {Che Chang} and Naik, {Nandita M.} and Kung, {Camy C.H.} and Shih, {Hsiu Ming} and Huang, {Tai Huang}",

note = "Funding Information: Acknowledgments This work is supported, in part, by Academia Sinica and by grants NSC 98-2113-M-001-014 (T.-H.H.) from the National Science Council of the Republic of China. The NMR spectra were obtained at the High-Field Nuclear Magnetic Resonance Center, Taiwan, which is supported by the National Research Program for Genomic Medicine, the Republic of China.",

year = "2011",

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doi = "10.1007/s12104-010-9271-4",

language = "English",

volume = "5",

pages = "75--77",

journal = "Biomolecular NMR Assignments",

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AU - Naik, Mandar T.

AU - Chang, Che Chang

AU - Naik, Nandita M.

AU - Kung, Camy C.H.

AU - Shih, Hsiu Ming

AU - Huang, Tai Huang

N1 - Funding Information: Acknowledgments This work is supported, in part, by Academia Sinica and by grants NSC 98-2113-M-001-014 (T.-H.H.) from the National Science Council of the Republic of China. The NMR spectra were obtained at the High-Field Nuclear Magnetic Resonance Center, Taiwan, which is supported by the National Research Program for Genomic Medicine, the Republic of China.

PY - 2011/4

Y1 - 2011/4

N2 - Small Ubiquitin-like MOdifiers (SUMOs) are ubiquitin-like proteins known to covalently modify large number of cellular proteins. The mammalian SUMO family includes four paralogues, SUMO-1 through SUMO-4. Death-associated protein-6, Daxx, is a 740 residue important transcription corepressor known to represses transcriptional potential of several sumolyted transcription factors. Daxx also plays important role in apoptosis. Both terminals of Daxx harbor separate SUMO Interaction Motifs (SIM), which mediate its interaction with SUMO and hence the sumolyted transcription factors. The C-terminal SIM of Daxx preferentially binds SUMO-1. Practically complete 1H, 13C and 15N resonance assignments for the complex between SUMO-1 and 20 residue Daxx C-terminal SIM peptide are reported here.

AB - Small Ubiquitin-like MOdifiers (SUMOs) are ubiquitin-like proteins known to covalently modify large number of cellular proteins. The mammalian SUMO family includes four paralogues, SUMO-1 through SUMO-4. Death-associated protein-6, Daxx, is a 740 residue important transcription corepressor known to represses transcriptional potential of several sumolyted transcription factors. Daxx also plays important role in apoptosis. Both terminals of Daxx harbor separate SUMO Interaction Motifs (SIM), which mediate its interaction with SUMO and hence the sumolyted transcription factors. The C-terminal SIM of Daxx preferentially binds SUMO-1. Practically complete 1H, 13C and 15N resonance assignments for the complex between SUMO-1 and 20 residue Daxx C-terminal SIM peptide are reported here.

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NMR chemical shift assignments of a complex between SUMO-1 and SIM peptide derived from the C-terminus of Daxx

Abstract

Keywords

ASJC Scopus subject areas

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