4clq
From Proteopedia
Structure of Rcl1p - Bms1p complex
Structural highlights
Function[RCL1_YEAST] Does not have cyclase activity. Plays a role in 40S-ribosomal-subunit biogenesis in the early pre-rRNA processing steps at sites A0, A1 and A2 that are required for proper maturation of the 18S RNA. Essential for viability. [BMS1_YEAST] May act as a molecular switch during maturation of the 40S ribosomal subunit in the nucleolus. The depletion of BMS1 interferes with processing of the 35S pre-rRNA at sites A0, A1, and A2, and the formation of 40S subunits.[1] [2] Publication Abstract from PubMedThe 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[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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