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4clq

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Revision as of 09:37, 4 August 2016

Structure of Rcl1p - Bms1p complex

Structural highlights

4clq is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 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^[3]

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

References

↑ Wegierski T, Billy E, Nasr F, Filipowicz W. Bms1p, a G-domain-containing protein, associates with Rcl1p and is required for 18S rRNA biogenesis in yeast. RNA. 2001 Sep;7(9):1254-67. PMID:11565748
↑ Gelperin D, Horton L, Beckman J, Hensold J, Lemmon SK. Bms1p, a novel GTP-binding protein, and the related Tsr1p are required for distinct steps of 40S ribosome biogenesis in yeast. RNA. 2001 Sep;7(9):1268-83. PMID:11565749
↑ Delprato A, Al Kadri Y, Perebaskine N, Monfoulet C, Henry Y, Henras AK, Fribourg S. Crucial role of the Rcl1p-Bms1p interaction for yeast pre-ribosomal RNA processing. Nucleic Acids Res. 2014;42(15):10161-72. doi: 10.1093/nar/gku682. Epub 2014 Jul, 26. PMID:25064857 doi:http://dx.doi.org/10.1093/nar/gku682

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4clq"

Categories: Fribourg, S | Translation

@@ Line 1: / Line 1: @@
 ==Structure of Rcl1p - Bms1p complex==
 <StructureSection load='4clq' size='340' side='right' caption='[[4clq]], [[Resolution|resolution]] 2.02&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[4clq]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CLQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CLQ FirstGlance]. <br>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4clq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4clq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4clq RCSB], [http://www.ebi.ac.uk/pdbsum/4clq PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4clq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4clq OCA], [http://pdbe.org/4clq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4clq RCSB], [http://www.ebi.ac.uk/pdbsum/4clq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4clq ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 16: / Line 17: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4clq" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4clq

From Proteopedia

Revision as of 09:37, 4 August 2016

Structure of Rcl1p - Bms1p complex

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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