4clq

Publication Abstract from PubMed

The essential Rcl1p and Bms1p proteins form a complex required for 40S ribosomal subunit maturation. Bms1p is a GTPase and Rcl1p has been proposed to catalyse the endonucleolytic cleavage at site A2 separating the pre-40S and pre-60S maturation pathways. We determined the 2.0 A crystal structure of Bms1p associated with Rcl1p. We demonstrate that Rcl1p nuclear import depends on Bms1p and that the two proteins are loaded into pre-ribosomes at a similar stage of the maturation pathway and remain present within pre-ribosomes after cleavage at A2. Importantly, GTP binding to Bms1p is not required for the import in the nucleus nor for the incorporation of Rcl1p into pre-ribosomes, but is essential for early pre-rRNA processing. We propose that GTP binding to Bms1p and/or GTP hydrolysis may induce conformational rearrangements within the Bms1p-Rcl1p complex allowing the interaction of Rcl1p with its RNA substrate.

Crucial role of the Rcl1p-Bms1p interaction for yeast pre-ribosomal RNA processing.,Delprato A, Al Kadri Y, Perebaskine N, Monfoulet C, Henry Y, Henras AK, Fribourg S Nucleic Acids Res. 2014;42(15):10161-72. doi: 10.1093/nar/gku682. Epub 2014 Jul, 26. PMID:25064857^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.