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Abstract
Ebp2p, the yeast homolog of human Epstein-Barr virus nuclear antigen 1-binding protein 2, is essential for biogenesis of the 60 S ribosomal subunit. Two-hybrid screening exhibited that, in addition to factors necessary for assembly of the 60 S subunit, Ebp2p interacts with Rps16p, ribosomal protein S16, and the 40 S ribosomal subunit assembly factor, Utp11p, as well as Yil019w, the function of which was previously uncharacterized. Depletion of Yil019w resulted in reduction in levels of both of 18 S rRNA and 40 S ribosomal subunit without affecting levels of 25 S rRNA and 60 S ribosomal subunits. 35 S pre-rRNA and aberrant 23 S RNA accumulated, indicating that pre-rRNA processing at sites A(0)-A(2) is inhibited when Yil019w is depleted. Each combination from Yil019w, Utp11p, and Rps16p showed two-hybrid interaction.
Highlights
Yeast ribosomes are composed of 4 rRNA and 78 ribosomal proteins
We demonstrate that YIL019w, named FAF1 (40 S assembly factor), encodes a novel factor essential for pre-rRNA processing and 40 S subunit assembly
Interaction of Ebp2p with Brx1p, Loc1p, or Ykl082c was detected by expression of the reporter gene HIS3 on SCϪLeu, Trp, His plates containing 5 mM 3-aminotriazole, but interaction of Ebp2p with Dbp9p, Nop12p, or Spb1p was on plates containing as low as 0.1–1 mM 3-aminotriazole. This two-hybrid screening revealed that Ebp2p interacts with Utp11p, a component of 90 S preribosomal particles [3], and Rps16p, a small ribosomal subunit protein
Summary
Yeast ribosomes are composed of 4 rRNA and 78 ribosomal proteins. Three mature (25, 18, and 5.8 S) rRNAs are synthesized as a long precursor, 35 S pre-rRNA, in the nucleolus [1, 2]. Thirty-five protein factors were identified by purification of the 90 S particle This complex is converted to precursors of the 40 and 60 S subunits by cleavage of the 35 S pre-rRNA at sites A0–A2 and assembly of other factors A combination of TAP purification and proteome analysis has revealed that many factors are required for pre-rRNA processing and assembly of 60 and 40 S subunits (5, 8 –12). These analyses suggested that the 90 S particle contains many 40 S assembly factors but few 60 S factors. We have shown that besides pre-rRNA processing and 60 S subunit assembly factors, Ebp2p interacts with Rps16p, ribosomal protein S16 (for nomenclature, see Ref. 15), and its associating factors, Utp11p and Yil019w. We demonstrate that YIL019w, named FAF1 (40 S assembly factor), encodes a novel factor essential for pre-rRNA processing and 40 S subunit assembly
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