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10.1016/j.molcel.2018.02.023 http://scihub22266oqcxt.onion/10.1016/j.molcel.2018.02.023 C5896202!5896202 !29576527     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=29576527 &cmd=llinks): Failed to open stream: HTTP request failed! 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Discovery and Characterization of ZUFSP/ZUP1, a Distinct Deubiquitinase Class Important for Genome Stability |pdf=|usr=}}{{29576527 }} gab.com Text Discovery and Characterization of ZUFSP/ZUP1, a Distinct Deubiquitinase Class Important for Genome Stability JO: Mol Cell http://www.kidney.de/pget.php?&tw=1&pmid=29576527 #FOAvip Deubiquitinating enzymes (DUBs) are important regulators of ubiquitin signaling. Here, we report the discovery of deubiquitinating activity in ZUFSP/C6orf113. High-resolution crystal structures of ZUFSP in complex with ubiquitin reveal several distinctive features of ubiquitin recognition and catalysis. Our analyses reveal that ZUFSP is a novel DUB with no homology to any known DUBs, leading us to classify ZUFSP as the seventh DUB family. Intriguingly, the minimal catalytic domain does not cleave polyubiquitin. We identify two ubiquitin binding domains in ZUFSP: a ZHA (ZUFSP helical arm) that binds to the distal ubiquitin and an atypical UBZ domain in ZUFSP that binds to polyubiquitin. Importantly, both domains are essential for ZUFSP to selectively cleave K63-linked polyubiquitin. We show that ZUFSP localizes to DNA lesions, where it plays an important role in genome stability pathways, functioning to prevent spontaneous DNA damage and also promote cellular survival in response to exogenous DNA damage. Twit Text FOAVip Discovery and Characterization of ZUFSP/ZUP1, a Distinct Deubiquitinase Class Important for Genome Stability ????Mol Cell http://www.kidney.de/pget.php?&tw=1&pmid=29576527 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29576527 #FOAvip English Wikipedia <ref>{{Cite pmid|29576527 }}</ref> Discovery and Characterization of ZUFSP/ZUP1, a Distinct Deubiquitinase Class Important for Genome Stability #MMPMID29576527 Kwasna D ; Abdul Rehman SA ; Natarajan J ; Matthews S ; Madden R ; De Cesare V ; Weidlich S ; Virdee S ; Ahel I ; Gibbs-Seymour I ; Kulathu Y Mol Cell 2018[Apr]; 70 (1 ): 150-164.e6 PMID29576527 show ga Deubiquitinating enzymes (DUBs) are important regulators of ubiquitin signaling. Here, we report the discovery of deubiquitinating activity in ZUFSP/C6orf113. High-resolution crystal structures of ZUFSP in complex with ubiquitin reveal several distinctive features of ubiquitin recognition and catalysis. Our analyses reveal that ZUFSP is a novel DUB with no homology to any known DUBs, leading us to classify ZUFSP as the seventh DUB family. Intriguingly, the minimal catalytic domain does not cleave polyubiquitin. We identify two ubiquitin binding domains in ZUFSP: a ZHA (ZUFSP helical arm) that binds to the distal ubiquitin and an atypical UBZ domain in ZUFSP that binds to polyubiquitin. Importantly, both domains are essential for ZUFSP to selectively cleave K63-linked polyubiquitin. We show that ZUFSP localizes to DNA lesions, where it plays an important role in genome stability pathways, functioning to prevent spontaneous DNA damage and also promote cellular survival in response to exogenous DNA damage. |*DNA Damage [MESH] |*Genomic Instability [MESH] |Binding Sites [MESH] |Cell Nucleus/*enzymology [MESH] |Cell Survival [MESH] |Deubiquitinating Enzymes/chemistry/genetics/*metabolism [MESH] |HEK293 Cells [MESH] |HeLa Cells [MESH] |Humans [MESH] |Jurkat Cells [MESH] |Lysine [MESH] |Polyubiquitin/*metabolism [MESH] |Protein Binding [MESH] |Protein Conformation [MESH] |Protein Interaction Domains and Motifs [MESH] |Structure-Activity Relationship [MESH] |Substrate Specificity [MESH]Discovery and Characterization of ZUFSP/ZUP1, a Distinct Deubiquitinas(epmc).pdf DeepDyve Pubget Overpricing