Characterizing the Conformational Dynamics of Human SUMO2: Insights into its Interaction with Metal Ions and SIMs.

Autor: Kaur A; Department of Chemistry, Guru Nanak Dev University, Amritsar, 143005, Punjab, India.; Present address: Institute for Bioscience and Biotechnology Research, University of Maryland & National Institute of Standards and Technology, United States., Singh H; Department of Chemistry, Guru Nanak Dev University, Amritsar, 143005, Punjab, India., Kumar D; Centre of Biomedical Research, Sanjay Gandhi Post-Graduate Institute of Medical Sciences Campus, Raebareli Road, Lucknow, 226014, Uttar Pradesh, India., Gahlay GK; Department of Molecular Biology and Biochemistry, Guru Nanak Dev University, Amritsar, 143005, Punjab, India., Mithu VS; Department of Chemistry, Guru Nanak Dev University, Amritsar, 143005, Punjab, India.; Present address: Department of NMR-based Structural Biology, Max Planck Institute for Multidisciplinary Sciences, Am Faßberg 11, Göttingen, 37077, Germany.
Jazyk: angličtina
Zdroj: Chembiochem : a European journal of chemical biology [Chembiochem] 2024 Jun 03; Vol. 25 (11), pp. e202400045. Date of Electronic Publication: 2024 May 10.
DOI: 10.1002/cbic.202400045
Abstrakt: SUMO (Small Ubiquitin-like Modifiers) proteins are involved in a crucial post-translational modification commonly termed as SUMOylation. In this work, we have investigated the native-state conformational flexibility of human SUMO2 and its interaction with Cu 2+ and Zn 2+ ions using 15 N- 1 H based 2D NMR spectroscopy. After SUMO1, SUMO2 is the most studied SUMO isoform in humans which shares 45 % and ~80 % similarity with SUMO1 in terms of sequence and structure, respectively. In this manuscript, we demonstrate that compared to SUMO1, several amino acids around the α 1 -helix region of SUMO2 access energetically similar near-native conformations. These conformations could play a crucial role in SUMO2's non-covalent interactions with SUMO interaction motifs (SIMs) on other proteins. The C-terminal of SUMO2 was found to bind strongly with Cu 2+ ions resulting in a trimeric structure as observed by gel electrophoresis. This interaction seems to interfere in its non-covalent interaction with a V/I-x-V/I-V/I based SIM in Daxx protein.
(© 2024 Wiley-VCH GmbH.)
Databáze: MEDLINE
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