4CLQ

Structure of Rcl1p - Bms1p complex

Summary for 4CLQ

• Entry DOI: 10.2210/pdb4clq/pdb
• Descriptor: RNA 3'-TERMINAL PHOSPHATE CYCLASE-LIKE PROTEIN, RIBOSOME BIOGENESIS PROTEIN BMS1 (3 entities in total)
• Functional Keywords: translation
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); More
• Cellular location: Nucleus, nucleolus: Q08096; Cytoplasm : Q08965
• Total number of polymer chains: 2
• Total formula weight: 51364.65

Authors

Fribourg, S. (deposition date: 2014-01-15, release date: 2014-11-26, Last modification date: 2024-10-23)

Primary citation

Delprato, A.,Al Kadri, Y.,Perebaskine, N.,Monfoulet, C.,Henry, Y.,Henras, A.K.,Fribourg, S.
Crucial Role of the Rcl1P-Bms1P Interaction for Yeast Pre-Ribosomal RNA Processing.
Nucleic Acids Res., 42:10161-, 2014

PubMed Abstract: 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 Å 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.

PubMed: 25064857
DOI: 10.1093/NAR/GKU682

Experimental method

X-RAY DIFFRACTION (2.02 Å)