7roz | pdb_00007roz

Structure of RNA-dependent RNA polymerase 2 (RDR2) from Arabidopsis thaliana

spinqualitylabelsall models 7roz, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7roz is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MG Activity: RNA-directed RNA polymerase, with EC number 2.7.7.48 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [RDR2_ARATH] RNA-dependent direct polymerase involved in the production of small interfering RNAs (siRNAs). Required for the biogenesis of endogenous siRNAs of 24 nucleotide which derive from heterochromatin and DNA repeats such as transposons or endogenous gene tandem repeats, such as repeats present in FWA gene. Involved in transcriptional gene silencing (TGS). Component of the RNA-directed DNA methylation (RdDM) silencing pathway that utilizes siRNAs to guide DNA methyltransferases to asymmetric cytosines. Involved in control of flowering time through RdDM of FWA locus. Required for reception of long-distance mRNA silencing in the shoot. Required for the formation of telomeric siRNAs and the RNA-dependent DNA methylation of asymmetric cytosines in telomeric (5'-CCCTAAA-3') repeats. Publication Abstract from PubMed RNA-dependent RNA polymerases play essential roles in RNA-mediated gene silencing in eukaryotes. In Arabidopsis, RNA-DEPENDENT RNA POLYMERASE 2 (RDR2) physically interacts with DNA-dependent NUCLEAR RNA POLYMERASE IV (Pol IV) and their activities are tightly coupled, with Pol IV transcriptional arrest, induced by the nontemplate DNA strand, somehow enabling RDR2 to engage Pol IV transcripts and generate double-stranded RNAs. The double-stranded RNAs are then released from the Pol IV-RDR2 complex and diced into short-interfering RNAs that guide RNA-directed DNA methylation and silencing. Here we report the structure of full-length RDR2, at an overall resolution of 3.1 A, determined by cryoelectron microscopy. The N-terminal region contains an RNA-recognition motif adjacent to a positively charged channel that leads to a catalytic center with striking structural homology to the catalytic centers of multisubunit DNA-dependent RNA polymerases. We show that RDR2 initiates 1 to 2 nt internal to the 3' ends of its templates and can transcribe the RNA of an RNA/DNA hybrid, provided that 9 or more nucleotides are unpaired at the RNA's 3' end. Using a nucleic acid configuration that mimics the arrangement of RNA and DNA strands upon Pol IV transcriptional arrest, we show that displacement of the RNA 3' end occurs as the DNA template and nontemplate strands reanneal, enabling RDR2 transcription. These results suggest a model in which Pol IV arrest and backtracking displaces the RNA 3' end as the DNA strands reanneal, allowing RDR2 to engage the RNA and synthesize the complementary strand. Structure and RNA template requirements of Arabidopsis RNA-DEPENDENT RNA POLYMERASE 2.,Fukudome A, Singh J, Mishra V, Reddem E, Martinez-Marquez F, Wenzel S, Yan R, Shiozaki M, Yu Z, Wang JC, Takagi Y, Pikaard CS Proc Natl Acad Sci U S A. 2021 Dec 21;118(51). pii: 2115899118. doi:, 10.1073/pnas.2115899118. PMID:34903670 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA