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| | ==NMR structure of the C-terminal RRM domain of poly(U) binding 1== | | ==NMR structure of the C-terminal RRM domain of poly(U) binding 1== |
| - | <StructureSection load='2la4' size='340' side='right'caption='[[2la4]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2la4' size='340' side='right'caption='[[2la4]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2la4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LA4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LA4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2la4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LA4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LA4 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PUB1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2la4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2la4 OCA], [https://pdbe.org/2la4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2la4 RCSB], [https://www.ebi.ac.uk/pdbsum/2la4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2la4 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=2la4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2la4 OCA], [https://pdbe.org/2la4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2la4 RCSB], [https://www.ebi.ac.uk/pdbsum/2la4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2la4 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/PUB1_YEAST PUB1_YEAST]] May be associated with hnRNA within the nucleus and remains associated during nucleocytoplasmic mRNA transport, once the proteins are in the cytoplasm, disassembly of PUB1-RNA complexes may occur prior to PAB1 binding and formation of a translationally competent RNP complex. Binds to polyadenylated RNA; prefers to bind poly(rU); binds to T-rich single-stranded DNA.
| + | [https://www.uniprot.org/uniprot/PUB1_YEAST PUB1_YEAST] May be associated with hnRNA within the nucleus and remains associated during nucleocytoplasmic mRNA transport, once the proteins are in the cytoplasm, disassembly of PUB1-RNA complexes may occur prior to PAB1 binding and formation of a translationally competent RNP complex. Binds to polyadenylated RNA; prefers to bind poly(rU); binds to T-rich single-stranded DNA. |
| | <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: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Martinez-Lumbreras, S]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Mirassou, Y]] | + | [[Category: Martinez-Lumbreras S]] |
| - | [[Category: Perez-Canadillas, J M]] | + | [[Category: Mirassou Y]] |
| - | [[Category: Rico-Lastres, P]] | + | [[Category: Perez-Canadillas JM]] |
| - | [[Category: Santiveri, C M]] | + | [[Category: Rico-Lastres P]] |
| - | [[Category: Nucleus]]
| + | [[Category: Santiveri CM]] |
| - | [[Category: Rna binding protein]]
| + | |
| - | [[Category: Rna recognition]]
| + | |
| - | [[Category: Rna-binding]]
| + | |
| - | [[Category: Rrm]]
| + | |
| - | [[Category: Stress granule]]
| + | |
| - | [[Category: Transcription]]
| + | |
| Structural highlights
Function
PUB1_YEAST May be associated with hnRNA within the nucleus and remains associated during nucleocytoplasmic mRNA transport, once the proteins are in the cytoplasm, disassembly of PUB1-RNA complexes may occur prior to PAB1 binding and formation of a translationally competent RNP complex. Binds to polyadenylated RNA; prefers to bind poly(rU); binds to T-rich single-stranded DNA.
Publication Abstract from PubMed
Pub1p, a highly abundant poly(A)+ mRNA binding protein in Saccharomyces cerevisiae, influences the stability and translational control of many cellular transcripts, particularly under some types of environmental stresses. We have studied the structure, RNA and protein recognition modes of different Pub1p constructs by NMR spectroscopy. The structure of the C-terminal RRM domain (RRM3) shows a non-canonical N-terminal helix that packs against the canonical RRM fold in an original fashion. This structural trait is conserved in Pub1p metazoan homologues, the TIA-1 family, defining a new class of RRM-type domains that we propose to name TRRM (TIA-1 C-terminal domain-like RRM). Pub1p TRRM and the N-terminal RRM1-RRM2 tandem bind RNA with high selectivity for U-rich sequences, with TRRM showing additional preference for UA-rich ones. RNA-mediated chemical shift changes map to beta-sheet and protein loops in the three RRMs. Additionally, NMR titration and biochemical in vitro cross-linking experiments determined that Pub1p TRRM interacts specifically with the N-terminal region (1-402) of yeast eIF4G1 (Tif4631p), very likely through the conserved Box1, a short sequence motif neighbouring the Pab1p binding site in Tif4631p. The interaction involves conserved residues of Pub1p TRRM, which define a protein interface that mirrors the Pab1p-Tif4631p binding mode. Neither protein nor RNA recognition involves the novel N-terminal helix, whose functional role remains unclear. By integrating these new results with the current knowledge about Pub1p, we proposed different mechanisms of Pub1p recruitment to the mRNPs and Pub1p-mediated mRNA stabilization in which the Pub1p/Tif4631p interaction would play an important role.
Pub1p C-terminal RRM domain interacts with Tif4631p through a conserved region neighbouring the Pab1p binding site.,Santiveri CM, Mirassou Y, Rico-Lastres P, Martinez-Lumbreras S, Perez-Canadillas JM PLoS One. 2011;6(9):e24481. Epub 2011 Sep 8. PMID:21931728[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Santiveri CM, Mirassou Y, Rico-Lastres P, Martinez-Lumbreras S, Perez-Canadillas JM. Pub1p C-terminal RRM domain interacts with Tif4631p through a conserved region neighbouring the Pab1p binding site. PLoS One. 2011;6(9):e24481. Epub 2011 Sep 8. PMID:21931728 doi:10.1371/journal.pone.0024481
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