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-Structure paper
タイトル | Structural analysis reveals the flexible C-terminus of Nop15 undergoes rearrangement to recognize a pre-ribosomal RNA folding intermediate. |
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ジャーナル・号・ページ | Nucleic Acids Res, Vol. 45, Issue 5, Page 2829-2837, Year 2017 |
掲載日 | 2017年3月17日 |
![]() | Jun Zhang / Lauren E Gonzalez / Traci M Tanaka Hall / ![]() |
PubMed 要旨 | The RNA recognition motif (RRM) is the most abundant RNA-binding domain in eukaryotes, and it plays versatile roles in RNA metabolism. Despite its abundance, diversity of RRM structure and function ...The RNA recognition motif (RRM) is the most abundant RNA-binding domain in eukaryotes, and it plays versatile roles in RNA metabolism. Despite its abundance, diversity of RRM structure and function is generated by variations on a conserved core. Yeast Nop15 is an RRM protein that is essential for large ribosomal subunit biogenesis. We determined a 2.0 Å crystal structure of Nop15 that reveals a C-terminal α-helical region obscures its canonical RNA-binding surface. Small-angle X-ray scattering, NMR and RNA-binding analyses further reveal that the C-terminal residues of Nop15 are highly flexible, but essential for tight RNA binding. Moreover, comparison with a recently reported cryo-electron microscopy structure indicates that dramatic rearrangement of the C-terminal region of Nop15 in the pre-ribosome exposes the RNA-binding surface to recognize the base of its stem-loop target RNA and extends a newly-formed α helix to the distal loop where it forms protein interactions. |
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手法 | SAS (X-ray synchrotron) / X線回折 |
解像度 | 2 Å |
構造データ | ![]() SASDBG6: ![]() PDB-5t9p: |
化合物 | ![]() ChemComp-SO4: ![]() ChemComp-CL: ![]() ChemComp-HOH: |
由来 |
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![]() | RIBOSOMAL PROTEIN / Nop15 / RRM |