N(6)-Adenine DNA-methyltransferase in wheat seedlings
The N(6)-adenine DNA-methyltransferase was isolated from the vacuolar vesicle fraction of wheat coleoptiles. In the presence of S-adenosyl-L-methionine the enzyme de novo methylates the first adenine residue in the TGATCA sequence in the single- or double-stranded DNA substrates but it prefers singl...
Gespeichert in:
Veröffentlicht in: | FEBS letters 2002-03, Vol.514 (2-3), p.305-308 |
---|---|
Hauptverfasser: | , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 308 |
---|---|
container_issue | 2-3 |
container_start_page | 305 |
container_title | FEBS letters |
container_volume | 514 |
creator | Fedoreyeva, Larisa I Vanyushin, Boris F |
description | The N(6)-adenine DNA-methyltransferase was isolated from the vacuolar vesicle fraction of wheat coleoptiles. In the presence of S-adenosyl-L-methionine the enzyme de novo methylates the first adenine residue in the TGATCA sequence in the single- or double-stranded DNA substrates but it prefers single-stranded structures. Wheat adenine DNA-methyltransferase (wadmtase) is a Mg(2+)- or Ca(2+)-dependent enzyme with a maximum activity at pH 7.5-8.0. Wadmtase seems to be responsible for mitochondrial DNA modification that might be involved in the regulation of replication of mitochondria in plants. |
doi_str_mv | 10.1016/S0014-5793(02)02384-0 |
format | Article |
fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_proquest_miscellaneous_71635064</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>71635064</sourcerecordid><originalsourceid>FETCH-LOGICAL-p122t-b9efc048d1d37d0d8a3052f36875f5c4e78fcb53a00699c25995f92686f650773</originalsourceid><addsrcrecordid>eNo9j8tOwzAURL0A0VL4BFBWqF0Yru34tYxaXlJVFsA6cuJrGpSkIU6E-vdUorAandHRSEPIFYNbBkzdvQKwlEptxRz4ArgwKYUTMv2vJ-Q8xk84sGH2jEwYs6lgmk2J3MzVgmYe26rFZLXJaIPDdl8PvWtjwN5FTKo2-d6iG5KI6Ouq_YgX5DS4OuLlMWfk_eH-bflE1y-Pz8tsTTvG-UALi6GE1HjmhfbgjRMgeRDKaBlkmaI2oSykcADK2pJLa2WwXBkVlAStxYzc_O52_e5rxDjkTRVLrGvX4m6MuWZKSFDpQbw-imPRoM-7vmpcv8__joof7N1Rpg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>71635064</pqid></control><display><type>article</type><title>N(6)-Adenine DNA-methyltransferase in wheat seedlings</title><source>MEDLINE</source><source>Wiley Online Library Journals Frontfile Complete</source><source>Elsevier ScienceDirect Journals</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>Wiley Free Content</source><source>Alma/SFX Local Collection</source><creator>Fedoreyeva, Larisa I ; Vanyushin, Boris F</creator><creatorcontrib>Fedoreyeva, Larisa I ; Vanyushin, Boris F</creatorcontrib><description>The N(6)-adenine DNA-methyltransferase was isolated from the vacuolar vesicle fraction of wheat coleoptiles. In the presence of S-adenosyl-L-methionine the enzyme de novo methylates the first adenine residue in the TGATCA sequence in the single- or double-stranded DNA substrates but it prefers single-stranded structures. Wheat adenine DNA-methyltransferase (wadmtase) is a Mg(2+)- or Ca(2+)-dependent enzyme with a maximum activity at pH 7.5-8.0. Wadmtase seems to be responsible for mitochondrial DNA modification that might be involved in the regulation of replication of mitochondria in plants.</description><identifier>ISSN: 0014-5793</identifier><identifier>DOI: 10.1016/S0014-5793(02)02384-0</identifier><identifier>PMID: 11943171</identifier><language>eng</language><publisher>England</publisher><subject>Calcium - pharmacology ; Chromatography, Gel ; Cytoplasmic Vesicles - chemistry ; Cytoplasmic Vesicles - enzymology ; DNA - chemistry ; DNA Methylation ; DNA, Mitochondrial - chemistry ; Electrophoresis, Polyacrylamide Gel ; Enzyme Activation - drug effects ; Hydrogen-Ion Concentration ; Magnesium - pharmacology ; Molecular Weight ; Oligonucleotides - chemistry ; Plant Proteins - chemistry ; Plant Proteins - isolation & purification ; Plant Shoots - chemistry ; Plant Shoots - enzymology ; Site-Specific DNA-Methyltransferase (Adenine-Specific) - chemistry ; Site-Specific DNA-Methyltransferase (Adenine-Specific) - isolation & purification ; Substrate Specificity ; Triticum - enzymology</subject><ispartof>FEBS letters, 2002-03, Vol.514 (2-3), p.305-308</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27903,27904</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11943171$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fedoreyeva, Larisa I</creatorcontrib><creatorcontrib>Vanyushin, Boris F</creatorcontrib><title>N(6)-Adenine DNA-methyltransferase in wheat seedlings</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>The N(6)-adenine DNA-methyltransferase was isolated from the vacuolar vesicle fraction of wheat coleoptiles. In the presence of S-adenosyl-L-methionine the enzyme de novo methylates the first adenine residue in the TGATCA sequence in the single- or double-stranded DNA substrates but it prefers single-stranded structures. Wheat adenine DNA-methyltransferase (wadmtase) is a Mg(2+)- or Ca(2+)-dependent enzyme with a maximum activity at pH 7.5-8.0. Wadmtase seems to be responsible for mitochondrial DNA modification that might be involved in the regulation of replication of mitochondria in plants.</description><subject>Calcium - pharmacology</subject><subject>Chromatography, Gel</subject><subject>Cytoplasmic Vesicles - chemistry</subject><subject>Cytoplasmic Vesicles - enzymology</subject><subject>DNA - chemistry</subject><subject>DNA Methylation</subject><subject>DNA, Mitochondrial - chemistry</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzyme Activation - drug effects</subject><subject>Hydrogen-Ion Concentration</subject><subject>Magnesium - pharmacology</subject><subject>Molecular Weight</subject><subject>Oligonucleotides - chemistry</subject><subject>Plant Proteins - chemistry</subject><subject>Plant Proteins - isolation & purification</subject><subject>Plant Shoots - chemistry</subject><subject>Plant Shoots - enzymology</subject><subject>Site-Specific DNA-Methyltransferase (Adenine-Specific) - chemistry</subject><subject>Site-Specific DNA-Methyltransferase (Adenine-Specific) - isolation & purification</subject><subject>Substrate Specificity</subject><subject>Triticum - enzymology</subject><issn>0014-5793</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9j8tOwzAURL0A0VL4BFBWqF0Yru34tYxaXlJVFsA6cuJrGpSkIU6E-vdUorAandHRSEPIFYNbBkzdvQKwlEptxRz4ArgwKYUTMv2vJ-Q8xk84sGH2jEwYs6lgmk2J3MzVgmYe26rFZLXJaIPDdl8PvWtjwN5FTKo2-d6iG5KI6Ouq_YgX5DS4OuLlMWfk_eH-bflE1y-Pz8tsTTvG-UALi6GE1HjmhfbgjRMgeRDKaBlkmaI2oSykcADK2pJLa2WwXBkVlAStxYzc_O52_e5rxDjkTRVLrGvX4m6MuWZKSFDpQbw-imPRoM-7vmpcv8__joof7N1Rpg</recordid><startdate>20020313</startdate><enddate>20020313</enddate><creator>Fedoreyeva, Larisa I</creator><creator>Vanyushin, Boris F</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>20020313</creationdate><title>N(6)-Adenine DNA-methyltransferase in wheat seedlings</title><author>Fedoreyeva, Larisa I ; Vanyushin, Boris F</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p122t-b9efc048d1d37d0d8a3052f36875f5c4e78fcb53a00699c25995f92686f650773</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Calcium - pharmacology</topic><topic>Chromatography, Gel</topic><topic>Cytoplasmic Vesicles - chemistry</topic><topic>Cytoplasmic Vesicles - enzymology</topic><topic>DNA - chemistry</topic><topic>DNA Methylation</topic><topic>DNA, Mitochondrial - chemistry</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Enzyme Activation - drug effects</topic><topic>Hydrogen-Ion Concentration</topic><topic>Magnesium - pharmacology</topic><topic>Molecular Weight</topic><topic>Oligonucleotides - chemistry</topic><topic>Plant Proteins - chemistry</topic><topic>Plant Proteins - isolation & purification</topic><topic>Plant Shoots - chemistry</topic><topic>Plant Shoots - enzymology</topic><topic>Site-Specific DNA-Methyltransferase (Adenine-Specific) - chemistry</topic><topic>Site-Specific DNA-Methyltransferase (Adenine-Specific) - isolation & purification</topic><topic>Substrate Specificity</topic><topic>Triticum - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fedoreyeva, Larisa I</creatorcontrib><creatorcontrib>Vanyushin, Boris F</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fedoreyeva, Larisa I</au><au>Vanyushin, Boris F</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>N(6)-Adenine DNA-methyltransferase in wheat seedlings</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>2002-03-13</date><risdate>2002</risdate><volume>514</volume><issue>2-3</issue><spage>305</spage><epage>308</epage><pages>305-308</pages><issn>0014-5793</issn><abstract>The N(6)-adenine DNA-methyltransferase was isolated from the vacuolar vesicle fraction of wheat coleoptiles. In the presence of S-adenosyl-L-methionine the enzyme de novo methylates the first adenine residue in the TGATCA sequence in the single- or double-stranded DNA substrates but it prefers single-stranded structures. Wheat adenine DNA-methyltransferase (wadmtase) is a Mg(2+)- or Ca(2+)-dependent enzyme with a maximum activity at pH 7.5-8.0. Wadmtase seems to be responsible for mitochondrial DNA modification that might be involved in the regulation of replication of mitochondria in plants.</abstract><cop>England</cop><pmid>11943171</pmid><doi>10.1016/S0014-5793(02)02384-0</doi><tpages>4</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0014-5793 |
ispartof | FEBS letters, 2002-03, Vol.514 (2-3), p.305-308 |
issn | 0014-5793 |
language | eng |
recordid | cdi_proquest_miscellaneous_71635064 |
source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Wiley Free Content; Alma/SFX Local Collection |
subjects | Calcium - pharmacology Chromatography, Gel Cytoplasmic Vesicles - chemistry Cytoplasmic Vesicles - enzymology DNA - chemistry DNA Methylation DNA, Mitochondrial - chemistry Electrophoresis, Polyacrylamide Gel Enzyme Activation - drug effects Hydrogen-Ion Concentration Magnesium - pharmacology Molecular Weight Oligonucleotides - chemistry Plant Proteins - chemistry Plant Proteins - isolation & purification Plant Shoots - chemistry Plant Shoots - enzymology Site-Specific DNA-Methyltransferase (Adenine-Specific) - chemistry Site-Specific DNA-Methyltransferase (Adenine-Specific) - isolation & purification Substrate Specificity Triticum - enzymology |
title | N(6)-Adenine DNA-methyltransferase in wheat seedlings |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-23T04%3A58%3A38IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=N(6)-Adenine%20DNA-methyltransferase%20in%20wheat%20seedlings&rft.jtitle=FEBS%20letters&rft.au=Fedoreyeva,%20Larisa%20I&rft.date=2002-03-13&rft.volume=514&rft.issue=2-3&rft.spage=305&rft.epage=308&rft.pages=305-308&rft.issn=0014-5793&rft_id=info:doi/10.1016/S0014-5793(02)02384-0&rft_dat=%3Cproquest_pubme%3E71635064%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=71635064&rft_id=info:pmid/11943171&rfr_iscdi=true |