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Structural studies of the yeast DNA damage-inducible protein Ddi1 reveal domain architecture of this eukaryotic protein family
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SYSNO ASEP 0464345 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Structural studies of the yeast DNA damage-inducible protein Ddi1 reveal domain architecture of this eukaryotic protein family Tvůrce(i) Trempe, J. F. (CA)
Grantz Šašková, Klára (UOCHB-X) RID, ORCID
Sivá, Monika (UOCHB-X) RID, ORCID
Ratcliffe, C. D. H. (CA)
Veverka, Václav (UOCHB-X) RID, ORCID
Hoegl, A. (CA)
Ménade, M. (CA)
Feng, X. (CA)
Shenker, S. (CA)
Svoboda, Michal (UOCHB-X) RID
Kožíšek, Milan (UOCHB-X) RID, ORCID
Konvalinka, Jan (UOCHB-X) RID, ORCID
Gehring, K. (CA)Číslo článku 33671 Zdroj.dok. Scientific Reports. - : Nature Publishing Group - ISSN 2045-2322
Roč. 6, Sep 20 (2016)Poč.str. 13 s. Jazyk dok. eng - angličtina Země vyd. GB - Velká Británie Klíč. slova ubiquitin-associated domains ; ray solution scattering ; torsion angle dynamics Vědní obor RIV CE - Biochemie CEP LK11205 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy LO1304 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy Institucionální podpora UOCHB-X - RVO:61388963 UT WOS 000383494400002 EID SCOPUS 84988592791 DOI 10.1038/srep33671 Anotace The eukaryotic Ddi1 family is defined by a conserved retroviral aspartyl protease-like (RVP) domain found in association with a ubiquitin-like (UBL) domain. Ddi1 from Saccharomyces cerevisiae additionally contains a ubiquitin-associated (UBA) domain. The substrate specificity and role of the protease domain in the biological functions of the Ddi family remain unclear. Yeast Ddi1 has been implicated in the regulation of cell cycle progression, DNA-damage repair, and exocytosis. Here, we investigated the multi-domain structure of yeast Ddi1 using X-ray crystallography, nuclear magnetic resonance, and small-angle X-ray scattering. The crystal structure of the RVP domain sheds light on a putative substrate recognition site involving a conserved loop. Isothermal titration calorimetry confirms that both UBL and UBA domains bind ubiquitin, and that Ddi1 binds K48-linked diubiquitin with enhanced affinity. The solution NMR structure of a helical domain that precedes the protease displays tertiary structure similarity to DNA-binding domains from transcription regulators. Our structural studies suggest that the helical domain could serve as a landing platform for substrates in conjunction with attached ubiquitin chains binding to the UBL and UBA domains. 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/srep33671
Počet záznamů: 1