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A lysine desert protects sumo-targeted Ub ligases from auto-ubiquitination and proteolysis to maintain genome stability in yeast
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Sharma, Pragati. A lysine desert protects sumo-targeted Ub ligases from auto-ubiquitination and proteolysis to maintain genome stability in yeast. Retrieved from https://doi.org/doi:10.7282/T36H4K31

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TitleA lysine desert protects sumo-targeted Ub ligases from auto-ubiquitination and proteolysis to maintain genome stability in yeast
NameSharma, Pragati (author); Brill, Steven J (chair); Madura, Kiran (internal member); Zaratiegui, Mikel (internal member); Gartenberg, Marc R (outside member); Rutgers University; Graduate School - New Brunswick
Date Created2015
Other Date2015-01 (degree)
SubjectBiochemistry, Lysine, Ubiquitin, Yeast
Extent1 online resource (ix, 128 p. : ill.)
DescriptionPost-translational modification by SUMO (Small Ubiquitin-like MOdifier) regulates the enzymatic activity, subcellular localization, and protein-protein interactions of modified target proteins. SUMO has also been implicated in proteasome-dependent protein degradation with the identification of a special class of enzymes termed, SUMO-Targeted Ubiquitin Ligases (STUbLs). These conserved enzymes typically possess multiple, tandem SUMO-Interaction Motifs and a RING domain that together facilitate the conjugation of ubiquitin to SUMO-modified target proteins. Originally discovered as essential gene pair for the viability of RecQ helicase-deficient yeast, SLX5 and SLX8 code for a heterodimeric STUbL. Two novel alleles of SLX5 were isolated in a forward genetic screen for suppressors of genome instability. A combination of genetic and biochemical experiments indicate that these alleles disrupt a conserved lysine desert, unique to STUbLs, leading to Slx5’s auto-ubiquitination and proteasome-mediated degradation. The results are consistent with the idea that STUbLs employ a lysine desert as a defense against self-destruction.
NotePh.D.
NoteIncludes bibliographical references
Noteby Pragati Sharma
Genretheses, ETD doctoral
Persistent URLhttps://doi.org/doi:10.7282/T36H4K31
Languageeng
CollectionGraduate School - New Brunswick Electronic Theses and Dissertations
Organization NameRutgers, The State University of New Jersey
RightsThe author owns the copyright to this work.
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