FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2016246105> ?p ?o ?g. }

• W2016246105 endingPage "128" @default.
• W2016246105 startingPage "124" @default.
• W2016246105 abstract "In Arabidopsis, the RNA-directed DNA methylation pathway is important for establishing and maintaining DNA methylation — here Pol V is shown to depend on SUVH2 and SUVH9, where both of these proteins are proposed to bind specifically to methylated DNA to recruit Pol V, providing a self-reinforcing loop mechanism for maintenance of RNA-directed DNA methylation. In the model plant Arabidopsis, the RNA-directed DNA methylation (RdDM) pathway is important for establishing and maintaining DNA methylation at genomic sites such as retrotransposons and heterochromatic repeats. The pathway involves two RNA polymerase complexes: Pol IV, which synthesizes small interfering RNAs, and Pol V, which generates non-coding transcripts that recruit downstream RdDM factors. Here, Steven Jacobsen and colleagues show that Pol V is dependent on two SRA/SET domain proteins, SUVH2 and SUVH9, for its activity and its recruitment to chromatin. SUVH2 and SUVH9 are proposed to bind specifically to methylated DNA in order to recruit Pol V, providing a self-reinforcing loop mechanism for maintenance of RdDM. This work suggests a mechanism for selectively targeting regions of plant genomes for epigenetic silencing. RNA-directed DNA methylation in Arabidopsis thaliana depends on the upstream synthesis of 24-nucleotide small interfering RNAs (siRNAs) by RNA POLYMERASE IV (Pol IV)1,2 and downstream synthesis of non-coding transcripts by Pol V. Pol V transcripts are thought to interact with siRNAs which then recruit DOMAINS REARRANGED METHYLTRANSFERASE 2 (DRM2) to methylate DNA3,4,5,6,7. The SU(VAR)3-9 homologues SUVH2 and SUVH9 act in this downstream step but the mechanism of their action is unknown8,9. Here we show that genome-wide Pol V association with chromatin redundantly requires SUVH2 and SUVH9. Although SUVH2 and SUVH9 resemble histone methyltransferases, a crystal structure reveals that SUVH9 lacks a peptide-substrate binding cleft and lacks a properly formed S-adenosyl methionine (SAM)-binding pocket necessary for normal catalysis, consistent with a lack of methyltransferase activity for these proteins8. SUVH2 and SUVH9 both contain SRA (SET- and RING-ASSOCIATED) domains capable of binding methylated DNA8, suggesting that they function to recruit Pol V through DNA methylation. Consistent with this model, mutation of DNA METHYLTRANSFERASE 1 (MET1) causes loss of DNA methylation, a nearly complete loss of Pol V at its normal locations, and redistribution of Pol V to sites that become hypermethylated. Furthermore, tethering SUVH2 with a zinc finger to an unmethylated site is sufficient to recruit Pol V and establish DNA methylation and gene silencing. These results indicate that Pol V is recruited to DNA methylation through the methyl-DNA binding SUVH2 and SUVH9 proteins, and our mechanistic findings suggest a means for selectively targeting regions of plant genomes for epigenetic silencing." @default.
• W2016246105 created "2016-06-24" @default.
• W2016246105 creator A5011670317 @default.
• W2016246105 creator A5016220698 @default.
• W2016246105 creator A5022262342 @default.
• W2016246105 creator A5022888501 @default.
• W2016246105 creator A5034027813 @default.
• W2016246105 creator A5054350125 @default.
• W2016246105 creator A5058024620 @default.
• W2016246105 creator A5065363214 @default.
• W2016246105 creator A5077706769 @default.
• W2016246105 creator A5079466619 @default.
• W2016246105 creator A5086958208 @default.
• W2016246105 creator A5087878008 @default.
• W2016246105 date "2014-01-22" @default.
• W2016246105 modified "2023-10-05" @default.
• W2016246105 title "SRA- and SET-domain-containing proteins link RNA polymerase V occupancy to DNA methylation" @default.
• W2016246105 cites W1539796472 @default.
• W2016246105 cites W1970891459 @default.
• W2016246105 cites W1971978509 @default.
• W2016246105 cites W1977063334 @default.
• W2016246105 cites W1978192207 @default.
• W2016246105 cites W1985629904 @default.
• W2016246105 cites W1985658587 @default.
• W2016246105 cites W1986191025 @default.
• W2016246105 cites W1989385772 @default.
• W2016246105 cites W1993257254 @default.
• W2016246105 cites W1999644599 @default.
• W2016246105 cites W2001224651 @default.
• W2016246105 cites W2002128513 @default.
• W2016246105 cites W2002815900 @default.
• W2016246105 cites W2007250559 @default.
• W2016246105 cites W2018503702 @default.
• W2016246105 cites W2018860787 @default.
• W2016246105 cites W2019525237 @default.
• W2016246105 cites W2026343134 @default.
• W2016246105 cites W2031297525 @default.
• W2016246105 cites W2059890127 @default.
• W2016246105 cites W2060273066 @default.
• W2016246105 cites W2067151470 @default.
• W2016246105 cites W2068634134 @default.
• W2016246105 cites W2070062215 @default.
• W2016246105 cites W2070062799 @default.
• W2016246105 cites W2081501916 @default.
• W2016246105 cites W2106473601 @default.
• W2016246105 cites W2123921804 @default.
• W2016246105 cites W2124026197 @default.
• W2016246105 cites W2133377110 @default.
• W2016246105 cites W2137015675 @default.
• W2016246105 cites W2139288600 @default.
• W2016246105 cites W2139581653 @default.
• W2016246105 cites W2147620906 @default.
• W2016246105 cites W2149691569 @default.
• W2016246105 cites W2161631109 @default.
• W2016246105 cites W2165941008 @default.
• W2016246105 cites W2166795672 @default.
• W2016246105 cites W2168780432 @default.
• W2016246105 cites W2180229411 @default.
• W2016246105 doi "https://doi.org/10.1038/nature12931" @default.
• W2016246105 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3963826" @default.
• W2016246105 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24463519" @default.
• W2016246105 hasPublicationYear "2014" @default.
• W2016246105 type Work @default.
• W2016246105 sameAs 2016246105 @default.
• W2016246105 citedByCount "251" @default.
• W2016246105 countsByYear W20162461052014 @default.
• W2016246105 countsByYear W20162461052015 @default.
• W2016246105 countsByYear W20162461052016 @default.
• W2016246105 countsByYear W20162461052017 @default.
• W2016246105 countsByYear W20162461052018 @default.
• W2016246105 countsByYear W20162461052019 @default.
• W2016246105 countsByYear W20162461052020 @default.
• W2016246105 countsByYear W20162461052021 @default.
• W2016246105 countsByYear W20162461052022 @default.
• W2016246105 countsByYear W20162461052023 @default.
• W2016246105 crossrefType "journal-article" @default.
• W2016246105 hasAuthorship W2016246105A5011670317 @default.
• W2016246105 hasAuthorship W2016246105A5016220698 @default.
• W2016246105 hasAuthorship W2016246105A5022262342 @default.
• W2016246105 hasAuthorship W2016246105A5022888501 @default.
• W2016246105 hasAuthorship W2016246105A5034027813 @default.
• W2016246105 hasAuthorship W2016246105A5054350125 @default.
• W2016246105 hasAuthorship W2016246105A5058024620 @default.
• W2016246105 hasAuthorship W2016246105A5065363214 @default.
• W2016246105 hasAuthorship W2016246105A5077706769 @default.
• W2016246105 hasAuthorship W2016246105A5079466619 @default.
• W2016246105 hasAuthorship W2016246105A5086958208 @default.
• W2016246105 hasAuthorship W2016246105A5087878008 @default.
• W2016246105 hasBestOaLocation W20162461052 @default.
• W2016246105 hasConcept C104317684 @default.
• W2016246105 hasConcept C150194340 @default.
• W2016246105 hasConcept C163002167 @default.
• W2016246105 hasConcept C190727270 @default.
• W2016246105 hasConcept C2756471 @default.
• W2016246105 hasConcept C41258723 @default.
• W2016246105 hasConcept C54355233 @default.
• W2016246105 hasConcept C552990157 @default.
• W2016246105 hasConcept C67705224 @default.

• next