Functional interaction in establishment of ribosomal integrity between small subunit protein rpS6 and translational regulator rpL10/Grc5p |
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Authors: | Pachler Karin Karl Thomas Kolmann Kerstin Mehlmer Norbert Eder Michaela Loeffler Michael Oender Kamil Hochleitner Elisabeth O Lottspeich Friedrich Bresgen Nikolaus Richter Klaus Breitenbach Michael Koller Lore |
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Institution: | Department of Cell Biology, Paris Lodron University Salzburg, Hellbrunnerstrasse 34, A-5020 Salzburg, Austria. |
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Abstract: | Functional ribosomes synthesize proteins in all living cells and are composed of two labile associated subunits, which are made of rRNA and ribosomal proteins. The rRNA of the small 40S subunit (SSU) of the functional eukaryotic 80S ribosome decodes the mRNA molecule and the large 60S subunit (LSU) rRNA catalyzes protein synthesis. Recent fine structure determinations of the ribosome renewed interest in the role of ribosomal proteins in modulation of the core ribosomal functions. RpL10/Grc5p is a component of the LSU and is a multifunctional translational regulator, operating in 60S subunit biogenesis, 60S subunit export and 60S subunit joining with the 40S subunit. Here, we report that rpL10/Grc5p functionally interacts with the nuclear export factor Nmd3p in modulation of the cellular polysome complement and with the small subunit protein rpS6 in subunit joining and differential protein expression. |
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Keywords: | Translational control Ribosomal protein rpL10/Grc5p rpS6 Differential protein expression |
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