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| | ==Structure and function of the N-terminal nucleolin binding domain of nuclear valocine containing protein like 2 (NVL2) harboring a nucleolar localization signal== | | ==Structure and function of the N-terminal nucleolin binding domain of nuclear valocine containing protein like 2 (NVL2) harboring a nucleolar localization signal== |
| - | <StructureSection load='2rre' size='340' side='right' caption='[[2rre]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2rre' size='340' side='right'caption='[[2rre]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2rre]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RRE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RRE FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2rre]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RRE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RRE FirstGlance]. <br> |
| - | </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=2rre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rre OCA], [http://pdbe.org/2rre PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2rre RCSB], [http://www.ebi.ac.uk/pdbsum/2rre PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2rre ProSAT]</span></td></tr> | + | </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=2rre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rre OCA], [https://pdbe.org/2rre PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rre RCSB], [https://www.ebi.ac.uk/pdbsum/2rre PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rre ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/NVL_MOUSE NVL_MOUSE] Participates in the assembly of the telomerase holoenzyme and effecting of telomerase activity via its interaction with TERT. Involved in both early and late stages of the pre-rRNA processing pathways. Spatiotemporally regulates 60S ribosomal subunit biogenesis in the nucleolus. Catalyzes the release of specific assembly factors, such as WDR74, from pre-60S ribosomal particles through the ATPase activity.[UniProtKB:O15381] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
| - | [[Category: Fujiwara, K]] | + | [[Category: Mus musculus]] |
| - | [[Category: Fujiwara, Y]] | + | [[Category: Fujiwara K]] |
| - | [[Category: Goda, N]] | + | [[Category: Fujiwara Y]] |
| - | [[Category: Hiroaki, H]] | + | [[Category: Goda N]] |
| - | [[Category: Iwaya, N]] | + | [[Category: Hiroaki H]] |
| - | [[Category: Shirakawa, M]] | + | [[Category: Iwaya N]] |
| - | [[Category: Tenno, T]] | + | [[Category: Shirakawa M]] |
| - | [[Category: Alternatively spliced domain]]
| + | [[Category: Tenno T]] |
| - | [[Category: Nuclear protein]]
| + | |
| - | [[Category: Nucleolar localization signal]]
| + | |
| - | [[Category: Rna binding]]
| + | |
| Structural highlights
Function
NVL_MOUSE Participates in the assembly of the telomerase holoenzyme and effecting of telomerase activity via its interaction with TERT. Involved in both early and late stages of the pre-rRNA processing pathways. Spatiotemporally regulates 60S ribosomal subunit biogenesis in the nucleolus. Catalyzes the release of specific assembly factors, such as WDR74, from pre-60S ribosomal particles through the ATPase activity.[UniProtKB:O15381]
Publication Abstract from PubMed
The N-terminal regions of AAA-ATPases (ATPase associated with various cellular activities) often contain a domain that defines the distinct functions of the enzymes, such as substrate specificity and subcellular localization. As described herein, we have determined the solution structure of an N-terminal unique domain isolated from nuclear valosin-containing protein (VCP)-like protein 2 (NVL2(UD)). NVL2(UD) contains three alpha helices with an organization resembling that of a winged helix motif, whereas a pair of beta-strands is missing. The structure is unique and distinct from those of other known type II AAA-ATPases, such as VCP. Consequently, we identified nucleolin from a HeLa cell extract as a binding partner of this domain. Nucleolin contains a long ( approximately 300 amino acids) intrinsically unstructured region, followed by the four tandem RNA recognition motifs and the C-terminal glycine/arginine-rich domain. Binding analyses revealed that NVL2(UD) potentially binds to any of the combinations of two successive RNA binding domains in the presence of RNA. Furthermore, NVL2(UD) has a characteristic loop, in which the key basic residues RRKR are exposed to the solvent at the edge of the molecule. The mutation study showed that these residues are necessary and sufficient for nucleolin-RNA complex binding as well as nucleolar localization. Based on the observations presented above, we propose that NVL2 serves as an unfoldase for the nucleolin-RNA complex. As inferred from its RNA dependence and its ATPase activity, NVL2 might facilitate the dissociation and recycling of nucleolin, thereby promoting efficient ribosome biogenesis.
Structure and function of the N-terminal nucleolin binding domain of nuclear valosin-containing protein-like 2 (NVL2) harboring a nucleolar localization signal.,Fujiwara Y, Fujiwara K, Goda N, Iwaya N, Tenno T, Shirakawa M, Hiroaki H J Biol Chem. 2011 Jun 17;286(24):21732-41. Epub 2011 Apr 7. PMID:21474449[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fujiwara Y, Fujiwara K, Goda N, Iwaya N, Tenno T, Shirakawa M, Hiroaki H. Structure and function of the N-terminal nucleolin binding domain of nuclear valosin-containing protein-like 2 (NVL2) harboring a nucleolar localization signal. J Biol Chem. 2011 Jun 17;286(24):21732-41. Epub 2011 Apr 7. PMID:21474449 doi:10.1074/jbc.M110.174680
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