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Publication Type : Journal Article
Publisher : Molecular and Cellular Biology
Source : Molecular and Cellular Biology, Volume 31, Number 11, p.2299-2310 (2011)
Keywords : article, Blotting, Carrier Proteins, Chromosomal Proteins, controlled study, crystallography, DNA repair, genomic instability, Humans, mass spectrometry, Models, Molecular, mutant, Mutation, Non-Histone, nonhuman, phenotype, priority journal, protein domain, protein function, Protein Structure, protein Ubc9, Quaternary, Schizosaccharomyces, Schizosaccharomyces pombe Proteins, signal transduction, Small Ubiquitin-Related Modifier Proteins, SUMO 2 protein, sumoylation, ubiquitin protein ligase E3, Ubiquitin-Conjugating Enzymes, Western, X-Ray
Campus : Amritapuri
School : School of Biotechnology
Center : Biotechnology
Department : biotechnology
Verified : Yes
Year : 2011
Abstract : Global sumoylation, SUMO chain formation, and genome stabilization are all outputs generated by a limited repertoire of enzymes. Mechanisms driving selectivity for each of these processes are largely uncharacterized. Here, through crystallographic analyses we show that the SUMO E2 Ubc9 forms a noncovalent complex with a SUMO-like domain of Rad60 (SLD2). Ubc9:SLD2 and Ubc9:SUMO noncovalent complexes are structurally analogous, suggesting that differential recruitment of Ubc9 by SUMO or Rad60 provides a novel means for such selectivity. Indeed, deconvoluting Ubc9 function by disrupting either the Ubc9:SLD2 or Ubc9:SUMO noncovalent complex reveals distinct roles in facilitating sumoylation. Ubc9:SLD2 acts in the Nse2 SUMO E3 ligase-dependent pathway for DNA repair, whereas Ubc9:SUMO instead promotes global sumoylation and chain formation, via the Pli1 E3 SUMO ligase. Moreover, this Pli1-dependent SUMO chain formation causes the genome instability phenotypes of SUMO-targeted ubiquitin ligase (STUbL) mutants. Overall, we determine that, unexpectedly, Ubc9 noncovalent partner choice dictates the role of sumoylation in distinct cellular pathways. © 2011, American Society for Microbiology. All Rights Reserved.
Cite this Research Publication : Ja Prudden, Perry, J. J. Pab, Nie, Ma, Vashisht, A. Ac, Arvai, A. Sa, Hitomi, Ca, Guenther, Ga, Wohlschlegel, J. Ac, Tainer, J. Aad, and Boddy, M. Na, “DNA repair and global sumoylation are regulated by distinct Ubc9 noncovalent complexes”, Molecular and Cellular Biology, vol. 31, pp. 2299-2310, 2011.