SUMO-Conjugating and SUMO-Deconjugating Enzymes from Arabidopsis [PDF]
Plant Physiology, 2006 Abstract Posttranslational protein modification by the small ubiquitin-like modifier (SUMO) is a highly dynamic and reversible process. To analyze the substrate specificity of SUMO-conjugating and -deconjugating enzymes from Arabidopsis (Arabidopsis thaliana), we reconstituted its SUMOylation cascade in vitro and tested the capacity of ...
Thomas Colby +3 more
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SUMO conjugating enzyme: a vital player of SUMO pathway in plants
Physiology and Molecular Biology of Plants, 2021 Plants face numerous challenges such as biotic and abiotic stresses during their whole lifecycle. As they are sessile in nature, they ought to develop multiple ways to act during stressed conditions to maintain cellular homeostasis. Among various defense mechanisms, the small ubiquitin-like modifiers (SUMO) pathway is considered as the most important ...
Shantwana Ghimire +6 more
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Non-covalent SUMO interactions with (de)conjugation enzymes. [PDF]
Essays BiochemSUMOylation – a protein post-translational modification (PTM) related to ubiquitylation – involves the reversible covalent attachment of the small ubiquitin-like modifier (SUMO) to proteins. During the conjugation and deconjugation cycle, SUMO is recognised and positioned by various enzymes through specific non-covalent interactions.
Cisse EH, Mishra A, Suskiewicz MJ.
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A Chemical and Enzymatic Approach to Study Site-Specific Sumoylation. [PDF]
PLoS ONE, 2015 A variety of cellular pathways are regulated by protein modifications with ubiquitin-family proteins. SUMO, the Small Ubiquitin-like MOdifier, is covalently attached to lysine on target proteins via a cascade reaction catalyzed by E1, E2, and E3 enzymes.
Claudio P Albuquerque +5 more
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Sumo E2 Enzyme UBC9 Is Required for Efficient Protein Quality Control in Cardiomyocytes [PDF]
Circulation Research, 2014 Rationale: Impairment of proteasomal function is pathogenic in several cardiac proteinopathies and can eventually lead to heart failure. Loss of proteasomal activity often results in the accumulation of large protein aggregates.
Manish Gupta +5 more
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Site-Specific Protein Ubiquitylation Using an Engineered, Chimeric E1 Activating Enzyme and E2 SUMO Conjugating Enzyme Ubc9 [PDF]
ACS Central Science, 2022 ISSN:2374 ...
Gaku Akimoto +2 more
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OsSCE1 Encoding SUMO E2-Conjugating Enzyme Involves in Drought Stress Response of Oryza sativa
Rice Science, 2018 Small ubiquitin-like modifier (SUMO)-conjugating enzymes are involved in post-translational regulatory processes in eukaryotes, including the conjugation of SUMO peptides to protein substrate (SUMOylation).
Dini Nurdiani +2 more
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Molecular mechanism of a covalent allosteric inhibitor of SUMO E1 activating enzyme [PDF]
Nature Communications, 2018 AbstractE1 enzymes activate ubiquitin (Ub) and ubiquitin-like modifiers (Ubls) in the first step of Ub/Ubl conjugation cascades and represent potential targets for therapeutic intervention in cancer and other life-threatening diseases. Here, we report the crystal structure of the E1 enzyme for the Ubl SUMO in complex with a recently discovered and ...
Zongyang Lv +9 more
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Human Proteoglycan Linkage Region Glycosyltransferases are Dimeric and Show Unexpected Specificities. [PDF]
Angew Chem Int Ed EnglNon‐canonical glycopeptides of the proteoglycan linkage region are accessible by the enzymes B3GalT6 and GlcAT‐1 confirming a recently discovered rescue mode in glycosaminoglycan (GAG) biosynthesis. The crystal structure of B3GalT6 revealed a covalent dimer linked by a disulfide. Abstract We selected the N,O‐glycosylated proteoglycan bikunin as a model
Weidler S +16 more
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Determine Interaction Affinity Changes of the SUMO E1 Activating Enzymes During SUMO Activation using Quantitative FRET technology [PDF]
Abstract The heterodimeric E1 complex, Aos1-Uba2, catalyzes the first adenylation activation of the SUMO1 peptide in the SUMOylation cascade. The reaction affinity and dynamics of the Aos1-Uba2 heterodimer during the first step activation have yet to be determined.
Ling Jiang +3 more
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