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| | ==Solution structure of the complex formed by the two N-terminal RNA-binding domains of nucleolin and a pre-rRNA target== | | ==Solution structure of the complex formed by the two N-terminal RNA-binding domains of nucleolin and a pre-rRNA target== |
| - | <StructureSection load='1rkj' size='340' side='right'caption='[[1rkj]], [[NMR_Ensembles_of_Models | 14 NMR models]]' scene=''> | + | <StructureSection load='1rkj' size='340' side='right'caption='[[1rkj]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1rkj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Golden_hamster Golden hamster]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RKJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RKJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1rkj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mesocricetus_auratus Mesocricetus auratus] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RKJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RKJ FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1fje|1fje]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NCL ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10036 Golden hamster])</td></tr>
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| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rkj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rkj OCA], [https://pdbe.org/1rkj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rkj RCSB], [https://www.ebi.ac.uk/pdbsum/1rkj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rkj ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1rkj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rkj OCA], [https://pdbe.org/1rkj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rkj RCSB], [https://www.ebi.ac.uk/pdbsum/1rkj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rkj ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/NUCL_MESAU NUCL_MESAU]] Nucleolin is the major nucleolar protein of growing eukaryotic cells. It is found associated with intranucleolar chromatin and pre-ribosomal particles. It induces chromatin decondensation by binding to histone H1. It is thought to play a role in pre-rRNA transcription and ribosome assembly. May play a role in the process of transcriptional elongation. Binds RNA oligonucleotides with 5'-UUAGGG-3' repeats more tightly than the telomeric single-stranded DNA 5'-TTAGGG-3' repeats (By similarity).<ref>PMID:3409881</ref>
| + | [https://www.uniprot.org/uniprot/NUCL_MESAU NUCL_MESAU] Nucleolin is the major nucleolar protein of growing eukaryotic cells. It is found associated with intranucleolar chromatin and pre-ribosomal particles. It induces chromatin decondensation by binding to histone H1. It is thought to play a role in pre-rRNA transcription and ribosome assembly. May play a role in the process of transcriptional elongation. Binds RNA oligonucleotides with 5'-UUAGGG-3' repeats more tightly than the telomeric single-stranded DNA 5'-TTAGGG-3' repeats (By similarity).<ref>PMID:3409881</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Golden hamster]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Feigon, J]] | + | [[Category: Mesocricetus auratus]] |
| - | [[Category: Finger, L D]] | + | [[Category: Mus musculus]] |
| - | [[Category: Johansson, C]] | + | [[Category: Feigon J]] |
| - | [[Category: Kim, S]] | + | [[Category: Finger LD]] |
| - | [[Category: Laird-Offringa, I A]] | + | [[Category: Johansson C]] |
| - | [[Category: Mueller, T D]] | + | [[Category: Kim S]] |
| - | [[Category: Trantirek, L]] | + | [[Category: Laird-Offringa IA]] |
| - | [[Category: Protein-rna complex]]
| + | [[Category: Mueller TD]] |
| - | [[Category: Rbd]] | + | [[Category: Trantirek L]] |
| - | [[Category: Transcription-rna complex]] | + | |
| Structural highlights
Function
NUCL_MESAU Nucleolin is the major nucleolar protein of growing eukaryotic cells. It is found associated with intranucleolar chromatin and pre-ribosomal particles. It induces chromatin decondensation by binding to histone H1. It is thought to play a role in pre-rRNA transcription and ribosome assembly. May play a role in the process of transcriptional elongation. Binds RNA oligonucleotides with 5'-UUAGGG-3' repeats more tightly than the telomeric single-stranded DNA 5'-TTAGGG-3' repeats (By similarity).[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Nucleolin is a 70 kDa multidomain protein involved in several steps of eukaryotic ribosome biogenesis. In vitro selection in combination with mutagenesis and structural analysis identified binding sites in pre-rRNA with the consensus (U/G)CCCG(A/G) in the context of a hairpin structure, the nucleolin recognition element (NRE). The central region of the protein contains four tandem RNA-binding domains (RBDs), of which the first two are responsible for the RNA-binding specificity and affinity for NREs. Here, we present the solution structure of the 28 kDa complex formed by the two N-terminal RNA-binding domains of nucleolin (RBD12) and a natural pre-rRNA target, b2NRE. The structure demonstrates that the sequence-specific recognition of the pre-rRNA NRE is achieved by intermolecular hydrogen bonds and stacking interactions involving mainly the beta-sheet surfaces of the two RBDs and the linker residues. A comparison with our previously determined NMR structure of RBD12 in complex with an in vitro selected RNA target, sNRE, shows that although the sequence-specific recognition of the loop consensus nucleotides is the same in the two complexes, they differ in several aspects. While the protein makes numerous specific contacts to the non-consensus nucleotides in the loop E motif (S-turn) in the upper part of the sNRE stem, nucleolin RBD12 contacts only consensus nucleotides in b2NRE. The absence of these upper stem contacts from the RBD12/b2NRE complex results in a much less stable complex, as demonstrated by kinetic analyses. The role of the loop E motif in high-affinity binding is supported by gel-shift analyses with a series of sNRE mutants. The less stable interaction of RBD12 with the natural RNA target is consistent with the proposed role of nucleolin as a chaperone that interacts transiently with pre-rRNA to prevent misfolding.
Solution structure of the complex formed by the two N-terminal RNA-binding domains of nucleolin and a pre-rRNA target.,Johansson C, Finger LD, Trantirek L, Mueller TD, Kim S, Laird-Offringa IA, Feigon J J Mol Biol. 2004 Apr 2;337(4):799-816. PMID:15033352[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Erard MS, Belenguer P, Caizergues-Ferrer M, Pantaloni A, Amalric F. A major nucleolar protein, nucleolin, induces chromatin decondensation by binding to histone H1. Eur J Biochem. 1988 Aug 15;175(3):525-30. PMID:3409881
- ↑ Johansson C, Finger LD, Trantirek L, Mueller TD, Kim S, Laird-Offringa IA, Feigon J. Solution structure of the complex formed by the two N-terminal RNA-binding domains of nucleolin and a pre-rRNA target. J Mol Biol. 2004 Apr 2;337(4):799-816. PMID:15033352 doi:http://dx.doi.org/10.1016/j.jmb.2004.01.056
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