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Crucial role of the Rcl1p-Bms1p interaction for yeast pre-ribosomal RNA processing.

Delprato A, Al Kadri Y, Pérébaskine N, Monfoulet C, Henry Y, Henras AK, Fribourg S - Nucleic Acids Res. (2014)

Bottom Line: 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.

View Article: PubMed Central - PubMed

Affiliation: Institut Européen de Chimie et Biologie, ARNA laboratory, Université de Bordeaux, F-33607 Pessac, France Institut National de la Santé Et de la Recherche Médicale, INSERM - U869, ARNA laboratory, F-33000 Bordeaux, France.

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Overall structure of Rcl1p–Bms1p core interacting domain. (A) Rcl1p can be described as three repeated domains (orange, pink and green) linked to a fourth distinct one (cyan). The Bms1p fragment is shown in deep blue. This and all subsequent structural figures were generated with PyMOL ((http://www.pymol.org). (B) Residues 547–569 of Bms1p form two short α-helices bound at the surface of Rcl1p domain 4. (C) Residues 606–636 of Bms1p extend over the four domains of Rcl1p and provide multiple contacts with Rcl1p.
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Figure 2: Overall structure of Rcl1p–Bms1p core interacting domain. (A) Rcl1p can be described as three repeated domains (orange, pink and green) linked to a fourth distinct one (cyan). The Bms1p fragment is shown in deep blue. This and all subsequent structural figures were generated with PyMOL ((http://www.pymol.org). (B) Residues 547–569 of Bms1p form two short α-helices bound at the surface of Rcl1p domain 4. (C) Residues 606–636 of Bms1p extend over the four domains of Rcl1p and provide multiple contacts with Rcl1p.

Mentions: The complex between full-length S. cerevisiae Rcl1p and Bms1p residues 1–705 was prepared and crystallized as described in the Materials and Methods section. Bms1p proteolysis occurred during sample preparation as visualized by Coomassie-blue staining of the purified and crystallized sample. Phases were obtained from a SAD data collection on Se-Met substituted Rcl1p (Supplementary Table S1 and Materials and Methods section). The structure was solved and refined to 20.18%/23.73% R-factor/R-free values at a resolution of 2.02 Å (Figure 2A).


Crucial role of the Rcl1p-Bms1p interaction for yeast pre-ribosomal RNA processing.

Delprato A, Al Kadri Y, Pérébaskine N, Monfoulet C, Henry Y, Henras AK, Fribourg S - Nucleic Acids Res. (2014)

Overall structure of Rcl1p–Bms1p core interacting domain. (A) Rcl1p can be described as three repeated domains (orange, pink and green) linked to a fourth distinct one (cyan). The Bms1p fragment is shown in deep blue. This and all subsequent structural figures were generated with PyMOL ((http://www.pymol.org). (B) Residues 547–569 of Bms1p form two short α-helices bound at the surface of Rcl1p domain 4. (C) Residues 606–636 of Bms1p extend over the four domains of Rcl1p and provide multiple contacts with Rcl1p.
© Copyright Policy - creative-commons
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4150785&req=5

Figure 2: Overall structure of Rcl1p–Bms1p core interacting domain. (A) Rcl1p can be described as three repeated domains (orange, pink and green) linked to a fourth distinct one (cyan). The Bms1p fragment is shown in deep blue. This and all subsequent structural figures were generated with PyMOL ((http://www.pymol.org). (B) Residues 547–569 of Bms1p form two short α-helices bound at the surface of Rcl1p domain 4. (C) Residues 606–636 of Bms1p extend over the four domains of Rcl1p and provide multiple contacts with Rcl1p.
Mentions: The complex between full-length S. cerevisiae Rcl1p and Bms1p residues 1–705 was prepared and crystallized as described in the Materials and Methods section. Bms1p proteolysis occurred during sample preparation as visualized by Coomassie-blue staining of the purified and crystallized sample. Phases were obtained from a SAD data collection on Se-Met substituted Rcl1p (Supplementary Table S1 and Materials and Methods section). The structure was solved and refined to 20.18%/23.73% R-factor/R-free values at a resolution of 2.02 Å (Figure 2A).

Bottom Line: 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.

View Article: PubMed Central - PubMed

Affiliation: Institut Européen de Chimie et Biologie, ARNA laboratory, Université de Bordeaux, F-33607 Pessac, France Institut National de la Santé Et de la Recherche Médicale, INSERM - U869, ARNA laboratory, F-33000 Bordeaux, France.

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