Open AccessFunctional interaction in establishment of ribosomal integrity between small subunit protein rpS6 and translational regulator rpL10/Grc5p
Author(s) -
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
Publication year - 2004
Publication title -
fems yeast research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.991
H-Index - 92
eISSN - 1567-1364
pISSN - 1567-1356
DOI - 10.1016/j.femsyr.2004.07.009
Subject(s) - eukaryotic small ribosomal subunit , eukaryotic large ribosomal subunit , eukaryotic ribosome , biology , ribosomal protein , protein subunit , ribosome , ribosome biogenesis , microbiology and biotechnology , ribosomal rna , polysome , genetics , rna , gene
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.