The Arabidopsis RNA-Binding Protein FCA Requires a Lysine-Specific Demethylase 1 Homolog to Downregulate FLC
A repressor of the transition to flowering in Arabidopsis is the MADS box protein FLOWERING LOCUS C (FLC). FCA, an RNA-binding protein, and FY, a homolog of the yeast RNA 3′ processing factor Pfs2p, downregulate FLC expression and therefore promote flowering. FCA/FY physically interact and alter pol...
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Veröffentlicht in: | Molecular cell 2007-11, Vol.28 (3), p.398-407 |
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description | A repressor of the transition to flowering in Arabidopsis is the MADS box protein FLOWERING LOCUS C (FLC). FCA, an RNA-binding protein, and FY, a homolog of the yeast RNA 3′ processing factor Pfs2p, downregulate FLC expression and therefore promote flowering. FCA/FY physically interact and alter polyadenylation/3′ processing to negatively autoregulate FCA. Here, we show that FCA requires FLOWERING LOCUS D (FLD), a homolog of the human lysine-specific demethylase 1 (LSD1) for FLC downregulation. FCA also partially depends on DICER-LIKE 3, involved in chromatin silencing. fca mutations increased levels of unspliced sense FLC transcript, altered processing of antisense FLC transcripts, and increased H3K4 dimethylation in the central region of FLC. These data support a close association of FCA and FLD in mediating H3K4 demethylation and thus transcriptional silencing of FLC and reveal roles for antisense RNA processing and DCL3 function in this regulation. |
doi_str_mv | 10.1016/j.molcel.2007.10.018 |
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FCA, an RNA-binding protein, and FY, a homolog of the yeast RNA 3′ processing factor Pfs2p, downregulate FLC expression and therefore promote flowering. FCA/FY physically interact and alter polyadenylation/3′ processing to negatively autoregulate FCA. Here, we show that FCA requires FLOWERING LOCUS D (FLD), a homolog of the human lysine-specific demethylase 1 (LSD1) for FLC downregulation. FCA also partially depends on DICER-LIKE 3, involved in chromatin silencing. fca mutations increased levels of unspliced sense FLC transcript, altered processing of antisense FLC transcripts, and increased H3K4 dimethylation in the central region of FLC. These data support a close association of FCA and FLD in mediating H3K4 demethylation and thus transcriptional silencing of FLC and reveal roles for antisense RNA processing and DCL3 function in this regulation.</description><identifier>ISSN: 1097-2765</identifier><identifier>EISSN: 1097-4164</identifier><identifier>DOI: 10.1016/j.molcel.2007.10.018</identifier><identifier>PMID: 17996704</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Arabidopsis - genetics ; Arabidopsis - metabolism ; Arabidopsis Proteins - chemistry ; Arabidopsis Proteins - genetics ; Arabidopsis Proteins - metabolism ; Arabidopsis Proteins - physiology ; Chromatin Immunoprecipitation ; DNA ; Down-Regulation ; Gene Silencing ; Histone Deacetylases - chemistry ; Histone Deacetylases - genetics ; Histone Deacetylases - physiology ; Histones - metabolism ; MADS Domain Proteins - chemistry ; MADS Domain Proteins - genetics ; MADS Domain Proteins - metabolism ; MADS Domain Proteins - physiology ; Methylation ; Molecular Sequence Data ; Mutation ; Ribonuclease III - metabolism ; RNA ; RNA Splicing ; RNA, Messenger - metabolism ; RNA-Binding Proteins - genetics ; RNA-Binding Proteins - metabolism ; RNA-Binding Proteins - physiology ; Signal Transduction ; Transcription, Genetic</subject><ispartof>Molecular cell, 2007-11, Vol.28 (3), p.398-407</ispartof><rights>2007 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c472t-78a2690b1c48b20cbe8361a5b22489d00ec36e25bf6749ffb9c92c66e26806af3</citedby><cites>FETCH-LOGICAL-c472t-78a2690b1c48b20cbe8361a5b22489d00ec36e25bf6749ffb9c92c66e26806af3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.molcel.2007.10.018$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>315,781,785,3551,27928,27929,45999</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17996704$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Liu, Fuquan</creatorcontrib><creatorcontrib>Quesada, Victor</creatorcontrib><creatorcontrib>Crevillén, Pedro</creatorcontrib><creatorcontrib>Bäurle, Isabel</creatorcontrib><creatorcontrib>Swiezewski, Szymon</creatorcontrib><creatorcontrib>Dean, Caroline</creatorcontrib><title>The Arabidopsis RNA-Binding Protein FCA Requires a Lysine-Specific Demethylase 1 Homolog to Downregulate FLC</title><title>Molecular cell</title><addtitle>Mol Cell</addtitle><description>A repressor of the transition to flowering in Arabidopsis is the MADS box protein FLOWERING LOCUS C (FLC). FCA, an RNA-binding protein, and FY, a homolog of the yeast RNA 3′ processing factor Pfs2p, downregulate FLC expression and therefore promote flowering. FCA/FY physically interact and alter polyadenylation/3′ processing to negatively autoregulate FCA. Here, we show that FCA requires FLOWERING LOCUS D (FLD), a homolog of the human lysine-specific demethylase 1 (LSD1) for FLC downregulation. FCA also partially depends on DICER-LIKE 3, involved in chromatin silencing. fca mutations increased levels of unspliced sense FLC transcript, altered processing of antisense FLC transcripts, and increased H3K4 dimethylation in the central region of FLC. These data support a close association of FCA and FLD in mediating H3K4 demethylation and thus transcriptional silencing of FLC and reveal roles for antisense RNA processing and DCL3 function in this regulation.</description><subject>Amino Acid Sequence</subject><subject>Arabidopsis - genetics</subject><subject>Arabidopsis - metabolism</subject><subject>Arabidopsis Proteins - chemistry</subject><subject>Arabidopsis Proteins - genetics</subject><subject>Arabidopsis Proteins - metabolism</subject><subject>Arabidopsis Proteins - physiology</subject><subject>Chromatin Immunoprecipitation</subject><subject>DNA</subject><subject>Down-Regulation</subject><subject>Gene Silencing</subject><subject>Histone Deacetylases - chemistry</subject><subject>Histone Deacetylases - genetics</subject><subject>Histone Deacetylases - physiology</subject><subject>Histones - metabolism</subject><subject>MADS Domain Proteins - chemistry</subject><subject>MADS Domain Proteins - genetics</subject><subject>MADS Domain Proteins - metabolism</subject><subject>MADS Domain Proteins - physiology</subject><subject>Methylation</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>Ribonuclease III - metabolism</subject><subject>RNA</subject><subject>RNA Splicing</subject><subject>RNA, Messenger - metabolism</subject><subject>RNA-Binding Proteins - genetics</subject><subject>RNA-Binding Proteins - metabolism</subject><subject>RNA-Binding Proteins - physiology</subject><subject>Signal Transduction</subject><subject>Transcription, Genetic</subject><issn>1097-2765</issn><issn>1097-4164</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kEtvGjEUha2qUUOT_IOq8qq7IbYxfmwqUQilEkorkqwtj-cOMZoZgz3Tin8fI5Cy6-peHZ1zHx9CXygZU0LF_W7chsZBM2aEyCyNCVUf0IgSLQtOBf946ZkU02v0OaUdIZRPlf6ErqnUWkjCR6h5fgU8i7b0Vdgnn_DmcVb88F3luy3-E0MPvsPL-Qxv4DD4CAlbvD4m30HxtAfna-_wAlroX4-NTYApXoV8V9jiPuBF-NdF2A6N7QEv1_NbdFXbJsHdpd6gl-XD83xVrH___DWfrQvHJesLqSwTmpTUcVUy4kpQE0HttGSMK10RAm4igE3LWkiu67rUTjMnsiQUEbae3KBv57n7GA4DpN60PmVUje0gDMkIxbViWmYjPxtdDClFqM0--tbGo6HEnCibnTlTNifKJzVTzrGvl_lD2UL1HrpgzYbvZwPkL_96iCY5D52DKiN0vamC__-GNy_pjy4</recordid><startdate>20071109</startdate><enddate>20071109</enddate><creator>Liu, Fuquan</creator><creator>Quesada, Victor</creator><creator>Crevillén, Pedro</creator><creator>Bäurle, Isabel</creator><creator>Swiezewski, Szymon</creator><creator>Dean, Caroline</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20071109</creationdate><title>The Arabidopsis RNA-Binding Protein FCA Requires a Lysine-Specific Demethylase 1 Homolog to Downregulate FLC</title><author>Liu, Fuquan ; Quesada, Victor ; Crevillén, Pedro ; Bäurle, Isabel ; Swiezewski, Szymon ; Dean, Caroline</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c472t-78a2690b1c48b20cbe8361a5b22489d00ec36e25bf6749ffb9c92c66e26806af3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Amino Acid Sequence</topic><topic>Arabidopsis - genetics</topic><topic>Arabidopsis - metabolism</topic><topic>Arabidopsis Proteins - chemistry</topic><topic>Arabidopsis Proteins - genetics</topic><topic>Arabidopsis Proteins - metabolism</topic><topic>Arabidopsis Proteins - physiology</topic><topic>Chromatin Immunoprecipitation</topic><topic>DNA</topic><topic>Down-Regulation</topic><topic>Gene Silencing</topic><topic>Histone Deacetylases - chemistry</topic><topic>Histone Deacetylases - genetics</topic><topic>Histone Deacetylases - physiology</topic><topic>Histones - metabolism</topic><topic>MADS Domain Proteins - chemistry</topic><topic>MADS Domain Proteins - genetics</topic><topic>MADS Domain Proteins - metabolism</topic><topic>MADS Domain Proteins - physiology</topic><topic>Methylation</topic><topic>Molecular Sequence Data</topic><topic>Mutation</topic><topic>Ribonuclease III - metabolism</topic><topic>RNA</topic><topic>RNA Splicing</topic><topic>RNA, Messenger - metabolism</topic><topic>RNA-Binding Proteins - genetics</topic><topic>RNA-Binding Proteins - metabolism</topic><topic>RNA-Binding Proteins - physiology</topic><topic>Signal Transduction</topic><topic>Transcription, Genetic</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Liu, Fuquan</creatorcontrib><creatorcontrib>Quesada, Victor</creatorcontrib><creatorcontrib>Crevillén, Pedro</creatorcontrib><creatorcontrib>Bäurle, Isabel</creatorcontrib><creatorcontrib>Swiezewski, Szymon</creatorcontrib><creatorcontrib>Dean, Caroline</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Liu, Fuquan</au><au>Quesada, Victor</au><au>Crevillén, Pedro</au><au>Bäurle, Isabel</au><au>Swiezewski, Szymon</au><au>Dean, Caroline</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Arabidopsis RNA-Binding Protein FCA Requires a Lysine-Specific Demethylase 1 Homolog to Downregulate FLC</atitle><jtitle>Molecular cell</jtitle><addtitle>Mol Cell</addtitle><date>2007-11-09</date><risdate>2007</risdate><volume>28</volume><issue>3</issue><spage>398</spage><epage>407</epage><pages>398-407</pages><issn>1097-2765</issn><eissn>1097-4164</eissn><abstract>A repressor of the transition to flowering in Arabidopsis is the MADS box protein FLOWERING LOCUS C (FLC). FCA, an RNA-binding protein, and FY, a homolog of the yeast RNA 3′ processing factor Pfs2p, downregulate FLC expression and therefore promote flowering. FCA/FY physically interact and alter polyadenylation/3′ processing to negatively autoregulate FCA. Here, we show that FCA requires FLOWERING LOCUS D (FLD), a homolog of the human lysine-specific demethylase 1 (LSD1) for FLC downregulation. FCA also partially depends on DICER-LIKE 3, involved in chromatin silencing. fca mutations increased levels of unspliced sense FLC transcript, altered processing of antisense FLC transcripts, and increased H3K4 dimethylation in the central region of FLC. These data support a close association of FCA and FLD in mediating H3K4 demethylation and thus transcriptional silencing of FLC and reveal roles for antisense RNA processing and DCL3 function in this regulation.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>17996704</pmid><doi>10.1016/j.molcel.2007.10.018</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence Arabidopsis - genetics Arabidopsis - metabolism Arabidopsis Proteins - chemistry Arabidopsis Proteins - genetics Arabidopsis Proteins - metabolism Arabidopsis Proteins - physiology Chromatin Immunoprecipitation DNA Down-Regulation Gene Silencing Histone Deacetylases - chemistry Histone Deacetylases - genetics Histone Deacetylases - physiology Histones - metabolism MADS Domain Proteins - chemistry MADS Domain Proteins - genetics MADS Domain Proteins - metabolism MADS Domain Proteins - physiology Methylation Molecular Sequence Data Mutation Ribonuclease III - metabolism RNA RNA Splicing RNA, Messenger - metabolism RNA-Binding Proteins - genetics RNA-Binding Proteins - metabolism RNA-Binding Proteins - physiology Signal Transduction Transcription, Genetic |
title | The Arabidopsis RNA-Binding Protein FCA Requires a Lysine-Specific Demethylase 1 Homolog to Downregulate FLC |
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