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Glycine-rich loop of mitochondrial processing peptidase α-subunit is responsible for substrate recognition by a mechanism analogous to mitochondrial receptor Tom20
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SYSNO ASEP 0340832 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Glycine-rich loop of mitochondrial processing peptidase α-subunit is responsible for substrate recognition by a mechanism analogous to mitochondrial receptor Tom20 Tvůrce(i) Dvořáková-Holá, Klára (MBU-M)
Matušková, Anna (MBU-M)
Kubala, M. (CZ)
Otyepka, M. (CZ)
Kučera, Tomáš (MBU-M)
Večeř, J. (CZ)
Heřman, P. (CZ)
Parkhomenko, Natalia (MBU-M) RID
Kutejová, E. (SK)
Janata, Jiří (MBU-M) RID, ORCIDZdroj.dok. Journal of Molecular Biology. - : Elsevier - ISSN 0022-2836
Roč. 396, č. 5 (2010), s. 1197-1210Poč.str. 14 s. Jazyk dok. eng - angličtina Země vyd. GB - Velká Británie Klíč. slova mitochondrial processing peptidase ; presequence ; substrate recognition Vědní obor RIV EE - Mikrobiologie, virologie CEP IAA501110631 GA AV ČR - Akademie věd CEZ AV0Z50200510 - MBU-M (2005-2011) UT WOS 000275691500002 DOI 10.1016/j.jmb.2009.12.054 Anotace Tryptophan fluorescence measurements were used to characterize the local dynamics of the highly conserved glycine-rich loop (GRL) of the mitochondrial processing peptidase (MPP) subunit in the presence of the substrate precursor. Reporter tryptophan residue was introduced into the GRL of the yeast MPP (Y299W) or at a proximal site (Y303W). Timeresolved and steady-state fluorescence spectroscopy demonstrated that for Trp299, the primary contact with the yeast malate dehydrogenase precursor evokes a change of the local GRL mobility. Moreover, time-resolved measurements showed that a functionless MPP with a single-residue deletion in the loop (Y303W/G292) is defective particularly in the primary contact with substrate Pracoviště Mikrobiologický ústav Kontakt Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Rok sběru 2011
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