GTPase-associated-center which is directly responsible for stimulation of translation-factor-dependent GTP hydrolysis belongs to the oldest and highly conserved ribosomal elements (1). In yeast cells proteins associated with that important part of ribosome are organised in pentameric complex P0-(P1-P2)2 (so called P-complex or “stalk”) (2) where N-terminal domain of ribosomal P0 protein acts as an anchor linking the stalk to the ribosome and directly interacting with the 26S rRNA, while C-terminal domain is responsible for binding of two P1/P2 heterodimers (3). Biogenesis of ribosome in eucariotic cell requires two transportation events: import to nucleus de novo synthesised ribosomal proteins and re-distribution of ribosomal subunits to cytoplasm. The major events in ribosome maturation process are well established, especially the maturation of 60S subunit is well understood where numerous trans acting factors which facilitate a maturation of the 60S subunit were identified (4). Assembly of the large ribosomal subunit require numerous factors and among them group of ribosomal like proteins (RLP) can be distinguished. In the biogenesis of ribosome RLP bind to rRNA in nucleolar compartment and subsequent maturation events are replaced by ribosomal proteins (5). Among pre-60S proteins, one so-called P0-like (RLPP0) was identified. It has N-terminal domain homologous to the N-terminal RNA-binding domain of bacterial/eukaryal L10 and P0 ribosomal proteins respectively and it may indicate that may take part in formation of the stalk, an event that is obscure so far during the ribosome maturation. On the basis of crystalographic 3D structure for prokaryotic L10, we perform in silico modelling of yeast and human RLPP0 proteins. We have constructed a hybrid proteins RLPP0-P0 where sequence coding the N-terminal rRNA binding domain of P0 protein was replaced by similar domain of RLPP0. We have found that plasmid-born expression of hybrid protein can support cell viability in lethal P0 null mutant genetic background, showing that both proteins RLPP0 and P0 bind to the same region of 26S rRNA. Our data provide additional data about the 60S ribosomal subunit maturation process, especially the problem of “stalk” formation is highlighted.

1. Rodnina, M. V., Stark, H., Savelsbergh, A., Wieden, H. J., Mohr, D., Matassova, N. B., Peske, F., Daviter, T., Gualerzi, C. O., and Wintermeyer, W. (2000) Biol Chem 381(5-6), 377-387

2. Tchorzewski, M. (2002) Int J Biochem Cell Biol 34(8), 911-915

3. Krokowski, D., Boguszewska, A., Abramczyk, D., Liljas, A., Tchorzewski, M., and Grankowski, N. (2006) Mol Microbiol 60(2), 386-400

4. Dez, C., and Tollervey, D. (2004) Curr Opin Microbiol 7(6), 631-637 5. Fatica, A., and Tollervey, D. (2002) Curr Opin Cell Biol 14(3), 313-318

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1. Structural Relationship Among Acidic Ribosomal Proteins From Three Phylogenetic Domains
2. Cellular Localization of The Human Acidic Ribosomal P proteins