Methylated DNA- binding proteins from arabidopsis
The 5-methylcytosines (m5C) play a critical role in epigenetic control, often being recognized by proteins containing a methyl-CpG-binding domain (MBD). Database screening has identified at least 12 putative methyl-CpG-binding proteins from Arabidopsis; we have isolated corresponding cDNAs for seven...
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description | The 5-methylcytosines (m5C) play a critical role in epigenetic control, often being recognized by proteins containing a methyl-CpG-binding domain (MBD). Database screening has identified at least 12 putative methyl-CpG-binding proteins from Arabidopsis; we have isolated corresponding cDNAs for seven of them. Despite variation in size and amino acid sequence, all seven proteins exclusively migrate into the nucleus as revealed by green fluorescent protein fusion protein assay, suggesting a relationship with chromatin structure. However, DNA-binding assays using bacterially expressed proteins and synthetic oligonucleotides containing m5C in CpGs showed only one to specifically bind, designated AtMBD5. Further analysis showed that AtMBD5 efficiently binds to m5C in CpNpN (N is A, T, or C) but not in CpNpG sequences, both frequently found in plant DNA. The other six proteins showed either nonspecific DNA binding or no ability to recognize m5C. RNA-blot hybridization and immunoblot analysis indicated AtMBD5 to be present essentially in all tissues. Using green fluorescent protein driven by the authentic promoter, AtMBD5 was found to be actively expressed in pistils and root tips. Because m5Cs in CpG and CpNpN are considered to function in gene expression and gene silencing, respectively, the present results suggest that AtMBD5 may have distinct functions in regulation and/or self defense of genes in actively proliferating cells. |
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Database screening has identified at least 12 putative methyl-CpG-binding proteins from Arabidopsis; we have isolated corresponding cDNAs for seven of them. Despite variation in size and amino acid sequence, all seven proteins exclusively migrate into the nucleus as revealed by green fluorescent protein fusion protein assay, suggesting a relationship with chromatin structure. However, DNA-binding assays using bacterially expressed proteins and synthetic oligonucleotides containing m5C in CpGs showed only one to specifically bind, designated AtMBD5. Further analysis showed that AtMBD5 efficiently binds to m5C in CpNpN (N is A, T, or C) but not in CpNpG sequences, both frequently found in plant DNA. The other six proteins showed either nonspecific DNA binding or no ability to recognize m5C. RNA-blot hybridization and immunoblot analysis indicated AtMBD5 to be present essentially in all tissues. Using green fluorescent protein driven by the authentic promoter, AtMBD5 was found to be actively expressed in pistils and root tips. Because m5Cs in CpG and CpNpN are considered to function in gene expression and gene silencing, respectively, the present results suggest that AtMBD5 may have distinct functions in regulation and/or self defense of genes in actively proliferating cells.</description><identifier>ISSN: 0032-0889</identifier><identifier>EISSN: 1532-2548</identifier><identifier>DOI: 10.1104/pp.103.026708</identifier><identifier>PMID: 14605234</identifier><identifier>CODEN: PPHYA5</identifier><language>eng</language><publisher>Rockville, MD: American Society of Plant Biologists</publisher><subject>5-methylcyosines ; Amino Acid Sequence ; Amino acids ; Arabidopsis ; Arabidopsis - genetics ; Arabidopsis - metabolism ; Arabidopsis Proteins - chemistry ; Arabidopsis Proteins - genetics ; Arabidopsis thaliana ; AtMBD5 protein ; binding sites ; Biological and medical sciences ; Birds ; Cell Biology and Signal Transduction ; cell nucleus ; Chromatin ; chromosome mapping ; Chromosomes ; Complementary DNA ; Conserved Sequence ; DNA ; DNA-binding proteins ; DNA-Binding Proteins - chemistry ; DNA-Binding Proteins - genetics ; Fundamental and applied biological sciences. Psychology ; Gels ; gene expression ; Genes ; Genes. Genome ; Methylation ; Molecular and cellular biology ; Molecular genetics ; Molecular Sequence Data ; molecular sequences data ; nucleotide sequences ; Phylogeny ; plant proteins ; Plants ; recombinant fusion proteins ; Sequence Alignment ; Sequence Homology, Amino Acid ; transgenic plants</subject><ispartof>Plant physiology (Bethesda), 2003-12, Vol.133 (4), p.1747-1754</ispartof><rights>Copyright 2003 American Society of Plant Biologists</rights><rights>2004 INIST-CNRS</rights><rights>Copyright © 2003, The American Society for Plant Biologists 2003</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c591t-beae5165649c556ae9448bb2b3dafdb8611865c7e7f0484f3669b826c7fff32c3</citedby><cites>FETCH-LOGICAL-c591t-beae5165649c556ae9448bb2b3dafdb8611865c7e7f0484f3669b826c7fff32c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/4281493$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/4281493$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,776,780,799,881,27901,27902,57992,58225</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=15380475$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14605234$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ho, M</creatorcontrib><creatorcontrib>Koike, A</creatorcontrib><creatorcontrib>Koizumi, N</creatorcontrib><creatorcontrib>Sano, H</creatorcontrib><title>Methylated DNA- binding proteins from arabidopsis</title><title>Plant physiology (Bethesda)</title><addtitle>Plant Physiol</addtitle><description>The 5-methylcytosines (m5C) play a critical role in epigenetic control, often being recognized by proteins containing a methyl-CpG-binding domain (MBD). Database screening has identified at least 12 putative methyl-CpG-binding proteins from Arabidopsis; we have isolated corresponding cDNAs for seven of them. Despite variation in size and amino acid sequence, all seven proteins exclusively migrate into the nucleus as revealed by green fluorescent protein fusion protein assay, suggesting a relationship with chromatin structure. However, DNA-binding assays using bacterially expressed proteins and synthetic oligonucleotides containing m5C in CpGs showed only one to specifically bind, designated AtMBD5. Further analysis showed that AtMBD5 efficiently binds to m5C in CpNpN (N is A, T, or C) but not in CpNpG sequences, both frequently found in plant DNA. The other six proteins showed either nonspecific DNA binding or no ability to recognize m5C. RNA-blot hybridization and immunoblot analysis indicated AtMBD5 to be present essentially in all tissues. Using green fluorescent protein driven by the authentic promoter, AtMBD5 was found to be actively expressed in pistils and root tips. Because m5Cs in CpG and CpNpN are considered to function in gene expression and gene silencing, respectively, the present results suggest that AtMBD5 may have distinct functions in regulation and/or self defense of genes in actively proliferating cells.</description><subject>5-methylcyosines</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Arabidopsis</subject><subject>Arabidopsis - genetics</subject><subject>Arabidopsis - metabolism</subject><subject>Arabidopsis Proteins - chemistry</subject><subject>Arabidopsis Proteins - genetics</subject><subject>Arabidopsis thaliana</subject><subject>AtMBD5 protein</subject><subject>binding sites</subject><subject>Biological and medical sciences</subject><subject>Birds</subject><subject>Cell Biology and Signal Transduction</subject><subject>cell nucleus</subject><subject>Chromatin</subject><subject>chromosome mapping</subject><subject>Chromosomes</subject><subject>Complementary DNA</subject><subject>Conserved Sequence</subject><subject>DNA</subject><subject>DNA-binding proteins</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>DNA-Binding Proteins - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gels</subject><subject>gene expression</subject><subject>Genes</subject><subject>Genes. Genome</subject><subject>Methylation</subject><subject>Molecular and cellular biology</subject><subject>Molecular genetics</subject><subject>Molecular Sequence Data</subject><subject>molecular sequences data</subject><subject>nucleotide sequences</subject><subject>Phylogeny</subject><subject>plant proteins</subject><subject>Plants</subject><subject>recombinant fusion proteins</subject><subject>Sequence Alignment</subject><subject>Sequence Homology, Amino Acid</subject><subject>transgenic plants</subject><issn>0032-0889</issn><issn>1532-2548</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkb1vFDEQxS0EIkegpEOwDXR7zPhr7YIiCp9SgAJSW16vfXG0t17sPaT89zjaUwIV1Tzp_WY0M4-Q5whbROBv53mLwLZAZQfqAdmgYLSlgquHZANQNSilT8iTUq4BABnyx-QEuQRBGd8Q_OqXq5vRLn5o3n87a5s-TkOcds2c0-LjVJqQ076x2fZxSHOJ5Sl5FOxY_LNjPSWXHz_8PP_cXnz_9OX87KJ1QuPS9t56gVJIrp0Q0nrNuep72rPBhqFXElFJ4TrfBeCKByal7hWVrgshMOrYKXm3zp0P_d4Pzk9LtqOZc9zbfGOSjeZfZ4pXZpd-GwbQUV373xz7c_p18GUx-1icH0c7-XQoprt9gsb_g9hpBKWhgu0KupxKyT7cLYNgbsMw81wlM2sYlX_59wX39PH7FXh9BGxxdgzZTi6We04wBbwTlXuxctdlSfnO51Qh16zar1Y72GTsLtcRlz9ozRpAsw4psD-M-KQ_</recordid><startdate>20031201</startdate><enddate>20031201</enddate><creator>Ho, M</creator><creator>Koike, A</creator><creator>Koizumi, N</creator><creator>Sano, H</creator><general>American Society of Plant Biologists</general><general>American Society of Plant Physiologists</general><general>The American Society for Plant Biologists</general><scope>FBQ</scope><scope>IQODW</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>7TM</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20031201</creationdate><title>Methylated DNA- binding proteins from arabidopsis</title><author>Ho, M ; Koike, A ; Koizumi, N ; Sano, H</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c591t-beae5165649c556ae9448bb2b3dafdb8611865c7e7f0484f3669b826c7fff32c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>5-methylcyosines</topic><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Arabidopsis</topic><topic>Arabidopsis - genetics</topic><topic>Arabidopsis - metabolism</topic><topic>Arabidopsis Proteins - chemistry</topic><topic>Arabidopsis Proteins - genetics</topic><topic>Arabidopsis thaliana</topic><topic>AtMBD5 protein</topic><topic>binding sites</topic><topic>Biological and medical sciences</topic><topic>Birds</topic><topic>Cell Biology and Signal Transduction</topic><topic>cell nucleus</topic><topic>Chromatin</topic><topic>chromosome mapping</topic><topic>Chromosomes</topic><topic>Complementary DNA</topic><topic>Conserved Sequence</topic><topic>DNA</topic><topic>DNA-binding proteins</topic><topic>DNA-Binding Proteins - chemistry</topic><topic>DNA-Binding Proteins - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gels</topic><topic>gene expression</topic><topic>Genes</topic><topic>Genes. Genome</topic><topic>Methylation</topic><topic>Molecular and cellular biology</topic><topic>Molecular genetics</topic><topic>Molecular Sequence Data</topic><topic>molecular sequences data</topic><topic>nucleotide sequences</topic><topic>Phylogeny</topic><topic>plant proteins</topic><topic>Plants</topic><topic>recombinant fusion proteins</topic><topic>Sequence Alignment</topic><topic>Sequence Homology, Amino Acid</topic><topic>transgenic plants</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ho, M</creatorcontrib><creatorcontrib>Koike, A</creatorcontrib><creatorcontrib>Koizumi, N</creatorcontrib><creatorcontrib>Sano, H</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Plant physiology (Bethesda)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ho, M</au><au>Koike, A</au><au>Koizumi, N</au><au>Sano, H</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Methylated DNA- binding proteins from arabidopsis</atitle><jtitle>Plant physiology (Bethesda)</jtitle><addtitle>Plant Physiol</addtitle><date>2003-12-01</date><risdate>2003</risdate><volume>133</volume><issue>4</issue><spage>1747</spage><epage>1754</epage><pages>1747-1754</pages><issn>0032-0889</issn><eissn>1532-2548</eissn><coden>PPHYA5</coden><abstract>The 5-methylcytosines (m5C) play a critical role in epigenetic control, often being recognized by proteins containing a methyl-CpG-binding domain (MBD). Database screening has identified at least 12 putative methyl-CpG-binding proteins from Arabidopsis; we have isolated corresponding cDNAs for seven of them. Despite variation in size and amino acid sequence, all seven proteins exclusively migrate into the nucleus as revealed by green fluorescent protein fusion protein assay, suggesting a relationship with chromatin structure. However, DNA-binding assays using bacterially expressed proteins and synthetic oligonucleotides containing m5C in CpGs showed only one to specifically bind, designated AtMBD5. Further analysis showed that AtMBD5 efficiently binds to m5C in CpNpN (N is A, T, or C) but not in CpNpG sequences, both frequently found in plant DNA. The other six proteins showed either nonspecific DNA binding or no ability to recognize m5C. RNA-blot hybridization and immunoblot analysis indicated AtMBD5 to be present essentially in all tissues. Using green fluorescent protein driven by the authentic promoter, AtMBD5 was found to be actively expressed in pistils and root tips. Because m5Cs in CpG and CpNpN are considered to function in gene expression and gene silencing, respectively, the present results suggest that AtMBD5 may have distinct functions in regulation and/or self defense of genes in actively proliferating cells.</abstract><cop>Rockville, MD</cop><pub>American Society of Plant Biologists</pub><pmid>14605234</pmid><doi>10.1104/pp.103.026708</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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source | Jstor Complete Legacy; Oxford University Press Journals All Titles (1996-Current); MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
subjects | 5-methylcyosines Amino Acid Sequence Amino acids Arabidopsis Arabidopsis - genetics Arabidopsis - metabolism Arabidopsis Proteins - chemistry Arabidopsis Proteins - genetics Arabidopsis thaliana AtMBD5 protein binding sites Biological and medical sciences Birds Cell Biology and Signal Transduction cell nucleus Chromatin chromosome mapping Chromosomes Complementary DNA Conserved Sequence DNA DNA-binding proteins DNA-Binding Proteins - chemistry DNA-Binding Proteins - genetics Fundamental and applied biological sciences. Psychology Gels gene expression Genes Genes. Genome Methylation Molecular and cellular biology Molecular genetics Molecular Sequence Data molecular sequences data nucleotide sequences Phylogeny plant proteins Plants recombinant fusion proteins Sequence Alignment Sequence Homology, Amino Acid transgenic plants |
title | Methylated DNA- binding proteins from arabidopsis |
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