2lrs: Difference between revisions
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==The second dsRBD domain from A. thaliana DICER-LIKE 1== | ==The second dsRBD domain from A. thaliana DICER-LIKE 1== | ||
<StructureSection load='2lrs' size='340' side='right' caption='[[2lrs]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2lrs' size='340' side='right' caption='[[2lrs]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
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<table><tr><td colspan='2'>[[2lrs]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LRS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LRS FirstGlance]. <br> | <table><tr><td colspan='2'>[[2lrs]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LRS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LRS FirstGlance]. <br> | ||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DCL1, ASU1, CAF SIN1, SUS1, At1g01040, T25K16.4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr> | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DCL1, ASU1, CAF SIN1, SUS1, At1g01040, T25K16.4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=2lrs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lrs OCA], [http://pdbe.org/2lrs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2lrs RCSB], [http://www.ebi.ac.uk/pdbsum/2lrs 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=2lrs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lrs OCA], [http://pdbe.org/2lrs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2lrs RCSB], [http://www.ebi.ac.uk/pdbsum/2lrs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2lrs ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == |
Revision as of 23:01, 1 August 2018
The second dsRBD domain from A. thaliana DICER-LIKE 1The second dsRBD domain from A. thaliana DICER-LIKE 1
Structural highlights
Function[DCL1_ARATH] Ribonuclease (RNase) III involved in RNA-mediated post-transcriptional gene silencing (PTGS). Functions in the microRNAs (miRNAs) biogenesis pathway by cleaving primary miRNAs (pri-miRNAs) and precursor miRNAs (pre-miRNAs). Functions with DRB1/HYL1 and SERRATE proteins for accurate pri-miRNAs to miRNAs processing. Indirectly involved in the production of trans-acting small interfering RNAs (ta-siRNAs) derived from the TAS1, TAS2 or TAS3 endogenous transcripts by participating in the production of their initiating miRNAs. Involved in the processing of natural siRNAs (nat-siRNAs, derived from cis-natural antisense transcripts) by cleaving 24 nucleotide nat-siRNAs into 21 nucleotide nat-siRNAs. Can produce RDR6-dependent endogenous ta-siRNAs derived from TAS1 and TAS2. Required for the production of 30-40 nucleotide bacterial-induced long siRNAs (lsiRNA). Acts redundantly with DICER-LIKE 3 (DCL3) to promote flowering via repression of FLOWERING LOCUS C (FLC). Represses antiviral RNA silencing through negative regulation of the expression of DCL4 and DCL3.[1] [2] [3] [4] [5] [6] [7] Publication Abstract from PubMedDicer-like ribonuclease III enzymes are involved in different paths related to RNA silencing in plants. Little is known about the structural aspects of these processes. Here we present a structural characterization of the second double-stranded RNA binding domain (dsRBD) of DCL1, which is presumed to participate in pri-micro-RNA recognition and subcellular localization of this protein. We determined the solution structure and found that it has a canonical fold but bears some variation with respect to other homologous domains. We also found that this domain binds both double-stranded RNA and double-stranded DNA, in contrast to most dsRBDs. Our characterization shows that this domain likely has functions other than substrate recognition and binding. Second Double-Stranded RNA Binding Domain of Dicer-like Ribonuclease 1: Structural and Biochemical Characterization.,Burdisso P, Suarez IP, Bologna NG, Palatnik JF, Bersch B, Rasia RM Biochemistry. 2012 Dec 21;51(51):10159-66. doi: 10.1021/bi301247r. Epub 2012 Dec , 12. PMID:23194006[8] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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