Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8322511 | The International Journal of Biochemistry & Cell Biology | 2015 | 22 Pages |
Abstract
Protein Mrt4 is one of trans-acting factors involved in ribosome biogenesis, which in higher eukaryotic cells contains a C-terminal extension similar to the C-terminal part of ribosomal P proteins. We show that human Mrt4 (hMrt4/MRTO4) undergoes phosphorylation in vivo and that serines S229, S233, and S235, placed within its acidic C-termini, have been phosphorylated by CK2 kinase in vitro. Such modification does not alter the subcellular distribution of hMrt4 in standard conditions but affects its molecular behavior during ActD induced nucleolar stress. Thus, we propose a new regulatory element important for the stress response pathway connecting ribosome biogenesis with cellular metabolism.
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Authors
Barbara Michalec-Wawiorka, Leszek Wawiorka, Kamil Derylo, Dawid Krokowski, Aleksandra Boguszewska, Eliza Molestak, Monika Szajwaj, Marek Tchorzewski,