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A large nucleolar U3 ribonucleoprotein required for 18S ribosomal RNA biogenesis
A large ribonucleoprotein (RNP) complex from Saccharomyces cerevisiae that contains the U3 snoRNA and 28 proteins is purified and it is suggested that this complex may correspond to the terminal knobs present at the 5′ ends of nascent pre-rRNAs.
Pre-18S ribosomal RNA is structurally compacted into the SSU processome prior to being cleaved from nascent transcripts in Saccharomyces cerevisiae.
RNA polymerase I transcription and pre-rRNA processing are linked by specific SSU processome components.
It is found that a subcomplex of SSU processome proteins, the t-Utps, is also required for optimal rRNA transcription in vivo in the yeast Saccharomyces cerevisiae.
The Putative NTPase Fap7 Mediates Cytoplasmic 20S Pre-rRNA Processing through a Direct Interaction with Rps14
- S. Granneman, M. R. Nandineni, S. Baserga
- Biology, ChemistryMolecular and Cellular Biology
- 1 December 2005
It is demonstrated that Fap7 is strictly required for cleavage of the 20S pre-rRNA at site D in the cytoplasm, consistent with an NTPase activity, and conserved residues predicted to be required for nucleoside triphosphate (NTP) hydrolysis are essential for Fap 7 function in vivo.
Ribosome Biogenesis in the Yeast Saccharomyces cerevisiae
Yeast ribosome biogenesis provide useful models for ribosomopathies, diseases in humans that result from failure to properly assemble ribosomes.
Imp3p and Imp4p, Two Specific Components of the U3 Small Nucleolar Ribonucleoprotein That Are Essential for Pre-18S rRNA Processing
Genetic depletion reveals that both Imp3p and Imp4p are critical for U3 snoRNP function in pre-18S rRNA processing at the A0, A1, and A2 sites in the pre-rRNA.
The Small-Subunit Processome Is a Ribosome Assembly Intermediate
- Kara A. Bernstein, J. Gallagher, B. M. Mitchell, S. Granneman, S. Baserga
- BiologyEukaryotic Cell
- 1 December 2004
12 additional protein components are characterized, including five small-ribosomal-subunit proteins and seven other proteins found to be bona fide SSU processome proteins that may be analogous to the primary or secondary RNA binding proteins first described in bacterial in vitro ribosome assembly maps.
The sigma(70)-like motif: a eukaryotic RNA binding domain unique to a superfamily of proteins required for ribosome biogenesis.
The initial U3 snoRNA:pre-rRNA base pairing interaction required for pre-18S rRNA folding revealed by in vivo chemical probing
The U3 snoRNP orchestrates the pre‐rRNA folding that results in the assembly of the small ribosomal subunit, and is required for the small subunit (SSU) processome formation.
The PINc domain protein Utp24, a putative nuclease, is required for the early cleavage steps in 18S rRNA maturation.
- F. Bleichert, S. Granneman, Y. Osheim, A. Beyer, S. Baserga
- BiologyProceedings of the National Academy of Sciences…
- 20 June 2006
This work examines the role of four previously uncharacterized PINc domain proteins, which are predicted to function as nucleases, in yeast ribosome biogenesis and suggests that Utp24 might be the elusive endonuclease that cleaves the pre-rRNA at sites A(1) and/or A(2.).