Počet záznamů: 1

Glycine-rich loop of mitochondrial processing peptidase α-subunit is responsible for substrate recognition by a mechanism analogous to mitochondrial receptor Tom20

  1. 1.
    0340832 - MBU-M 2011 RIV GB eng J - Článek v odborném periodiku
    Dvořáková-Holá, Klára - Matušková, Anna - Kubala, M. - Otyepka, M. - Kučera, Tomáš - Večeř, J. - Heřman, P. - Parkhomenko, Natalia - Kutejová, E. - Janata, Jiří
    Glycine-rich loop of mitochondrial processing peptidase α-subunit is responsible for substrate recognition by a mechanism analogous to mitochondrial receptor Tom20.
    Journal of Molecular Biology. Roč. 396, č. 5 (2010), s. 1197-1210 ISSN 0022-2836
    Grant CEP: GA AV ČR IAA501110631
    Výzkumný záměr: CEZ:AV0Z50200510
    Klíčová slova: mitochondrial processing peptidase * presequence * substrate recognition
    Kód oboru RIV: EE - Mikrobiologie, virologie
    Impakt faktor: 4.008, rok: 2010

    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
    Trvalý link: http://hdl.handle.net/11104/0183995