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Human DNA-Damage-Inducible 2 Protein Is Structurally and Functionally Distinct from Its Yeast Ortholog
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SYSNO ASEP 0463511 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Human DNA-Damage-Inducible 2 Protein Is Structurally and Functionally Distinct from Its Yeast Ortholog Tvůrce(i) Sivá, Monika (UOCHB-X) RID, ORCID
Svoboda, Michal (UOCHB-X) RID
Veverka, Václav (UOCHB-X) RID, ORCID
Trempe, J. F. (CA)
Hofmann, K. (DE)
Kožíšek, Milan (UOCHB-X) RID, ORCID
Hexnerová, Rozálie (UOCHB-X) ORCID, RID
Sedlák, František (UOCHB-X) RID, ORCID
Belza, Jan (UOCHB-X)
Brynda, Jiří (UOCHB-X) RID, ORCID
Šácha, Pavel (UOCHB-X) RID, ORCID
Hubálek, Martin (UOCHB-X) RID, ORCID
Starková, Jana (UOCHB-X)
Flaisigová, Iva (UOCHB-X)
Konvalinka, Jan (UOCHB-X) RID, ORCID
Grantz Šašková, Klára (UOCHB-X) RID, ORCIDČíslo článku 30443 Zdroj.dok. Scientific Reports. - : Nature Publishing Group - ISSN 2045-2322
Roč. 6, Jul 27 (2016)Poč.str. 15 s. Jazyk dok. eng - angličtina Země vyd. GB - Velká Británie Klíč. slova human DNA-damage-inducible 2 protein ; proteasome ; ubiquitin ; retroviral protease-like domain Vědní obor RIV CE - Biochemie CEP GBP208/12/G016 GA ČR - Grantová agentura ČR Institucionální podpora UOCHB-X - RVO:61388963 UT WOS 000380331500001 EID SCOPUS 84980002308 DOI 10.1038/srep30443 Anotace Although Ddi1-like proteins are conserved among eukaryotes, their biological functions remain poorly characterized. Yeast Ddi1 has been implicated in cell cycle regulation, DNA-damage response, and exocytosis. By virtue of its ubiquitin-like (UBL) and ubiquitin-associated (UBA) domains, it has been proposed to serve as a proteasomal shuttle factor. All Ddi1-like family members also contain a highly conserved retroviral protease-like (RVP) domain with unknown substrate specificity. While the structure and biological function of yeast Ddi1 have been investigated, no such analysis is available for the human homologs. To address this, we solved the 3D structures of the human Ddi2 UBL and RVP domains and identified a new helical domain that extends on either side of the RVP dimer. While Ddi1-like proteins from all vertebrates lack a UBA domain, we identify a novel ubiquitin-interacting motif (UIM) located at the C-terminus of the protein. The UIM showed a weak yet specific affinity towards ubiquitin, as did the Ddi2 UBL domain. However, the full-length Ddi2 protein is unable to bind to di-ubiquitin chains. While proteomic analysis revealed no activity, implying that the protease requires other factors for activation, our structural characterization of all domains of human Ddi2 sets the stage for further characterization. Pracoviště Ústav organické chemie a biochemie Kontakt asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Viktorie Chládková, Tel.: 232 002 434 Rok sběru 2017 Elektronická adresa http://www.nature.com/articles/srep30443
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