Topic
Ribosomes catalyze the translation of mRNA into proteins. Thereby, they have a key role in gene expression, cell growth and cell cycle progression. Ribosomes are large ribonucleo-protein complexes (RNP’s) consisting of ribosomal RNA (rRNA) and a large number (>50) of ribosomal proteins (r-proteins). Recent years brought detailed insights into the 3D-organisation of rRNA and r-proteins in mature ribosomes. In addition, it became evident that a significant proportion of the genome of an unicellular eukaryote (bakers yeast S. cerevisiae) codes for factors which are required for making ribosomes. Taking yeast as model system, we use a variety of in vivo and in vitro approaches to study the interrelationship between important processes in eukaryotic ribosome biogenesis, namely RNA synthesis, RNA processing, RNA folding, RNP assembly, and intracellular transport of RNP precursors.
Team
Joachim Griesenbeck, Principal investigatoremail: joachim.griesenbeck (at) ur.de | |
Philipp Milkereit, Principal investigatoremail: philipp.milkereit (at) ur.de | |
Gisela Pöll, Technical assistantemail: gisela.poell (at) ur.de | |
Herbert Tschochner, Principal investigatoremail: herbert.tschochner (at) ur.de |
PubLications
Selected publications
Linnemann, J., Pöll, G., Jakob, S., Ferreira-Cerca, S., Griesenbeck, J., Tschochner, H., and Milkereit, P. (2019). Impact of two neighbouring ribosomal protein clusters on biogenesis factor binding and assembly of yeast late small ribosomal subunit precursors. PloS One 14, e0203415.
Pöll, G., Müller, C., Bodden, M., Teubl, F., Eichner, N., Lehmann, G., Griesenbeck, J., Tschochner, H., and Milkereit, P. (2017). Structural transitions during large ribosomal subunit maturation analyzed by tethered nuclease structure probing in S. cerevisiae. PloS One 12, e0179405.
Ohmayer, U., Gil-Hernández, Á., Sauert, M., Martín-Marcos, P., Tamame, M., Tschochner, H., Griesenbeck, J., and Milkereit, P. (2015). Studies on the Coordination of Ribosomal Protein Assembly Events Involved in Processing and Stabilization of Yeast Early Large Ribosomal Subunit Precursors. PloS One 10, e0143768.
Ohmayer, U., Gamalinda, M., Sauert, M., Ossowski, J., Pöll, G., Linnemann, J., Hierlmeier, T., Perez-Fernandez, J., Kumcuoglu, B., Leger-Silvestre, I., Faubladier, M., Griesenbeck, J., Woolford, J., Tschochner, H., and Milkereit, P. (2013). Studies on the Assembly Characteristics of Large Subunit Ribosomal Proteins in S. cerevisae. PloS One 8, e68412.
Hierlmeier, T., Merl, J., Sauert, M., Perez-Fernandez, J., Schultz, P., Bruckmann, A., Hamperl, S., Ohmayer, U., Rachel, R., Jacob, A., Hergert, K., Deutzmann, R., Griesenbeck, J., Hurt, E., Milkereit, P., Baßler, J., and Tschochner, H. (2013). Rrp5p, Noc1p and Noc2p form a protein module which is part of early large ribosomal subunit precursors in S. cerevisiae. Nucleic Acids Res. 41, 1191–1210.
Jakob, S., Ohmayer, U., Neueder, A., Hierlmeier, T., Perez-Fernandez, J., Hochmuth, E., Deutzmann, R., Griesenbeck, J., Tschochner, H., Milkereit, P. (2012). Interrelationships between Yeast Ribosomal Protein Assembly Events and Transient Ribosome Biogenesis Factors Interactions in Early Pre-Ribosomes. PLoS ONE 7, e32552.
Ohmayer, U., Perez-Fernandez, J., Hierlmeier, T., Pöll, G., Williams, L., Griesenbeck, J., Tschochner, H., Milkereit, P. (2012). Local tertiary structure probing of ribonucleoprotein particles by nuclease fusion proteins. PLoS ONE 7, e42449.
Jakovljevic, J., Ohmayer, U., Gamalinda, M., Talkish, J., Alexander, L., Linnemann, J., Milkereit, P., and Woolford, J.L. (2012). Ribosomal proteins L7 and L8 function in concert with six A₃ assembly factors to propagate assembly of domains I and II of 25S rRNA in yeast 60S ribosomal subunits. RNA N. Y. N 18, 1805–1822.
A local role for the small ribosomal subunit primary binder rpS5 in final 18S rRNA processing in yeast.
Neueder A, Jakob S, Pöll G, Linnemann J, Deutzmann R, Tschochner H, Milkereit P. PLoS One. 2010 Apr 19;5(4):e10194.
Analysis of ribosome biogenesis factor-modules in yeast cells depleted from pre-ribosomes. Merl J, Jakob S, Ridinger K, Hierlmeier T, Deutzmann R, Milkereit P, Tschochner H. Nucleic Acids Res. 2010 May;38(9):3068-80. Epub 2010 Jan 25.
The Noc-domain containing C-terminus of Noc4p mediates both formation of the Noc4p-Nop14p submodule and its incorporation into the SSU processome. Kühn H, Hierlmeier T, Merl J, Jakob S, Aguissa-Touré AH, Milkereit P, Tschochner H. PLoS One. 2009 Dec 18;4(12):e8370.
rRNA maturation in yeast cells depleted of large ribosomal subunit proteins. Pöll G, Braun T, Jakovljevic J, Neueder A, Jakob S, Woolford JL Jr, Tschochner H, Milkereit P. PLoS One. 2009 Dec 11;4(12):e8249.
Analysis of the in vivo assembly pathway of eukaryotic 40S ribosomal proteins. Ferreira-Cerca S, Pöll G, Kühn H, Neueder A, Jakob S, Tschochner H, Milkereit P. Mol Cell. 2007 Nov 9;28(3):446-57.
Roles of eukaryotic ribosomal proteins in maturation and transport of pre-18S rRNA and ribosome function. Ferreira-Cerca S, Pöll G, Gleizes PE, Tschochner H, Milkereit P. Mol Cell. 2005 Oct 28;20(2):263-75.
The pre-ribosomal network. Milkereit P, Kühn H, Gas N, Tschochner H. Nucleic Acids Res. 2003 Feb 1;31(3):799-804.
A Noc complex specifically involved in the formation and nuclear export of ribosomal 40 S subunits. Milkereit P, Strauss D, Bassler J, Gadal O, Kühn H, Schütz S, Gas N, Lechner J, Hurt E, Tschochner H. J Biol Chem. 2003 Feb 7;278(6):4072-81. Epub 2002 Nov 20.
Maturation and intranuclear transport of pre-ribosomes requires Noc proteins. Milkereit P, Gadal O, Podtelejnikov A, Trumtel S, Gas N, Petfalski E, Tollervey D, Mann M, Hurt E, Tschochner H. Cell. 2001 May 18;105(4):499-509.
Association of yeast RNA polymerase I with a nucleolar substructure active in rRNA synthesis and processing. Fath S, Milkereit P, Podtelejnikov AV, Bischler N, Schultz P, Bier M, Mann M, Tschochner H. J Cell Biol. 2000 May 1;149(3):575-90.
All relevant publications in PubMed.
Funding
-
since July 2011
DFG collaborative research Center SFB960 at the University of Regensburg: Ribosome formation: principles of RNP biogenesis and control of their function
Project B1: Analyses of eukaryotic ribosome assembly