DNA binding mediated by the wheat HMGa protein: a novel instance of selectivity against alternating GC sequence
Identifieur interne : 000074 ( Istex/Corpus ); précédent : 000073; suivant : 000075DNA binding mediated by the wheat HMGa protein: a novel instance of selectivity against alternating GC sequence
Auteurs : Chua Yii Leng ; Pwee Keng Hock ; R. Manjunatha KiniSource :
- Plant Molecular Biology [ 0167-4412 ] ; 2001-05-01.
English descriptors
- KwdEn :
Abstract
Abstract: The high-mobility-group (HMG) chromosomal protein wheat HMGa was purified to homogeneity and tested for its binding characteristics to double-stranded DNA. Wheat HMGa was able to bind to P268, an A/T-rich fragment derived from the pea plastocyanin gene promoter, producing a small mobility shift in gel retardation assays where the bound complex was sensitive to addition of proteinase K but resistant to heat treatment of the protein, consistent with the identity of wheat HMGa as a putative HMG-I/Y protein. Gel retardation assays and southwestern hybridization analysis revealed that wheat HMGa could selectively interact with the DNA polynucleotides poly(dA).poly(dT), poly(dAdT).poly(dAdT), and poly(dG).poly(dC), but not with poly(dGdC).poly(dGdC). Surface plasmon resonance analysis determined the kinetic and affinity constants of sensor chip-immobilized wheat HMGa for double-stranded DNA 10-mers, revealing a good affinity of the protein for various dinucleotide combinations, except that of alternating GC sequence. Thus contrary to prior reports of a selectivity of wheat HMGa for A/T-rich DNA, the protein appears to be able to interact with sequences containing guanine and cytosine residues as well, except where G/C residues alternate directly in the primary sequence.
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DOI: 10.1023/A:1010696604330
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Manjunatha Kini</name><affiliation><mods:affiliation>Department of Biological Sciences, National University of Singapore, Block S1A, 10 Science Drive 4, 117543, Singapore, Republic of Singapore</mods:affiliation></affiliation></author></analytic><monogr></monogr><series><title level="j">Plant Molecular Biology</title><title level="j" type="sub">An International Journal on Molecular Biology, Molecular Genetics and Biochemistry</title><title level="j" type="abbrev">Plant Mol Biol</title><idno type="ISSN">0167-4412</idno><idno type="eISSN">1573-5028</idno><imprint><publisher>Kluwer Academic Publishers</publisher><pubPlace>Dordrecht</pubPlace><date type="published" when="2001-05-01">2001-05-01</date><biblScope unit="volume">46</biblScope><biblScope unit="issue">2</biblScope><biblScope unit="page" from="193">193</biblScope><biblScope unit="page" to="204">204</biblScope></imprint><idno type="ISSN">0167-4412</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0167-4412</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>A/T-rich</term><term>G/C-rich</term><term>high-mobility-group (HMG) proteins</term><term>southwestern hybridization</term><term>surface plasmon resonance analysis</term><term>wheat HMGa</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The high-mobility-group (HMG) chromosomal protein wheat HMGa was purified to homogeneity and tested for its binding characteristics to double-stranded DNA. Wheat HMGa was able to bind to P268, an A/T-rich fragment derived from the pea plastocyanin gene promoter, producing a small mobility shift in gel retardation assays where the bound complex was sensitive to addition of proteinase K but resistant to heat treatment of the protein, consistent with the identity of wheat HMGa as a putative HMG-I/Y protein. Gel retardation assays and southwestern hybridization analysis revealed that wheat HMGa could selectively interact with the DNA polynucleotides poly(dA).poly(dT), poly(dAdT).poly(dAdT), and poly(dG).poly(dC), but not with poly(dGdC).poly(dGdC). Surface plasmon resonance analysis determined the kinetic and affinity constants of sensor chip-immobilized wheat HMGa for double-stranded DNA 10-mers, revealing a good affinity of the protein for various dinucleotide combinations, except that of alternating GC sequence. Thus contrary to prior reports of a selectivity of wheat HMGa for A/T-rich DNA, the protein appears to be able to interact with sequences containing guanine and cytosine residues as well, except where G/C residues alternate directly in the primary sequence.</div></front></TEI><istex><corpusName>springer-journals</corpusName><author><json:item><name>Chua Yii Leng</name><affiliations><json:string>Plant Molecular Biology Laboratory, Singapore</json:string></affiliations></json:item><json:item><name>Pwee Keng Hock</name><affiliations><json:string>Plant Molecular Biology Laboratory, Singapore</json:string></affiliations></json:item><json:item><name>R. Manjunatha Kini</name><affiliations><json:string>Department of Biological Sciences, National University of Singapore, Block S1A, 10 Science Drive 4, 117543, Singapore, Republic of Singapore</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>A/T-rich</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>G/C-rich</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>high-mobility-group (HMG) proteins</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>surface plasmon resonance analysis</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>southwestern hybridization</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>wheat HMGa</value></json:item></subject><articleId><json:string>336196</json:string><json:string>Art7</json:string></articleId><arkIstex>ark:/67375/VQC-8VRKBZR7-D</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>OriginalPaper</json:string></originalGenre><abstract>Abstract: The high-mobility-group (HMG) chromosomal protein wheat HMGa was purified to homogeneity and tested for its binding characteristics to double-stranded DNA. Wheat HMGa was able to bind to P268, an A/T-rich fragment derived from the pea plastocyanin gene promoter, producing a small mobility shift in gel retardation assays where the bound complex was sensitive to addition of proteinase K but resistant to heat treatment of the protein, consistent with the identity of wheat HMGa as a putative HMG-I/Y protein. Gel retardation assays and southwestern hybridization analysis revealed that wheat HMGa could selectively interact with the DNA polynucleotides poly(dA).poly(dT), poly(dAdT).poly(dAdT), and poly(dG).poly(dC), but not with poly(dGdC).poly(dGdC). Surface plasmon resonance analysis determined the kinetic and affinity constants of sensor chip-immobilized wheat HMGa for double-stranded DNA 10-mers, revealing a good affinity of the protein for various dinucleotide combinations, except that of alternating GC sequence. Thus contrary to prior reports of a selectivity of wheat HMGa for A/T-rich DNA, the protein appears to be able to interact with sequences containing guanine and cytosine residues as well, except where G/C residues alternate directly in the primary sequence.</abstract><qualityIndicators><score>9.184</score><pdfWordCount>6820</pdfWordCount><pdfCharCount>41616</pdfCharCount><pdfVersion>1.3</pdfVersion><pdfPageCount>12</pdfPageCount><pdfPageSize>595 x 842 pts (A4)</pdfPageSize><refBibsNative>false</refBibsNative><abstractWordCount>182</abstractWordCount><abstractCharCount>1294</abstractCharCount><keywordCount>6</keywordCount></qualityIndicators><title>DNA binding mediated by the wheat HMGa protein: a novel instance of selectivity against alternating GC sequence</title><genre><json:string>research-article</json:string></genre><host><title>Plant Molecular 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Leng</surname></persName><affiliation>Plant Molecular Biology Laboratory, Singapore</affiliation></author><author xml:id="author-0001"><persName><forename type="first">Pwee</forename><surname>Keng Hock</surname></persName><affiliation>Plant Molecular Biology Laboratory, Singapore</affiliation></author><author xml:id="author-0002"><persName><forename type="first">R.</forename><surname>Kini</surname></persName><affiliation>Department of Biological Sciences, National University of Singapore, Block S1A, 10 Science Drive 4, 117543, Singapore, Republic of Singapore</affiliation></author><idno type="istex">CEC1471031E22FD0AA4A4F4D4E074363743AE8CF</idno><idno type="ark">ark:/67375/VQC-8VRKBZR7-D</idno><idno type="DOI">10.1023/A:1010696604330</idno><idno type="article-id">336196</idno><idno type="article-id">Art7</idno></analytic><monogr><title level="j">Plant Molecular Biology</title><title level="j" type="sub">An International Journal on Molecular Biology, Molecular Genetics and 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Wheat HMGa was able to bind to P268, an A/T-rich fragment derived from the pea plastocyanin gene promoter, producing a small mobility shift in gel retardation assays where the bound complex was sensitive to addition of proteinase K but resistant to heat treatment of the protein, consistent with the identity of wheat HMGa as a putative HMG-I/Y protein. Gel retardation assays and southwestern hybridization analysis revealed that wheat HMGa could selectively interact with the DNA polynucleotides poly(dA).poly(dT), poly(dAdT).poly(dAdT), and poly(dG).poly(dC), but not with poly(dGdC).poly(dGdC). Surface plasmon resonance analysis determined the kinetic and affinity constants of sensor chip-immobilized wheat HMGa for double-stranded DNA 10-mers, revealing a good affinity of the protein for various dinucleotide combinations, except that of alternating GC sequence. Thus contrary to prior reports of a selectivity of wheat HMGa for A/T-rich DNA, the protein appears to be able to interact with sequences containing guanine and cytosine residues as well, except where G/C residues alternate directly in the primary sequence.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><item><term>A/T-rich</term></item><item><term>G/C-rich</term></item><item><term>high-mobility-group (HMG) proteins</term></item><item><term>surface plasmon resonance analysis</term></item><item><term>southwestern hybridization</term></item><item><term>wheat HMGa</term></item></list></keywords></textClass><textClass><keywords scheme="Journal Subject"><list><head>Life Sciences</head><item><term>Biochemistry, general</term></item><item><term>Plant Sciences</term></item><item><term>Plant Pathology</term></item></list></keywords></textClass></profileDesc><revisionDesc><change 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Molecular Biology</JournalTitle><JournalSubTitle>An International Journal on Molecular Biology, Molecular Genetics and Biochemistry</JournalSubTitle><JournalAbbreviatedTitle>Plant Mol Biol</JournalAbbreviatedTitle><JournalSubjectGroup><JournalSubject Type="Primary">Life Sciences</JournalSubject><JournalSubject Type="Secondary">Biochemistry, general</JournalSubject><JournalSubject Type="Secondary">Plant Sciences</JournalSubject><JournalSubject Type="Secondary">Plant Pathology</JournalSubject></JournalSubjectGroup></JournalInfo><Volume><VolumeInfo VolumeType="Regular" TocLevels="0"><VolumeIDStart>46</VolumeIDStart><VolumeIDEnd>46</VolumeIDEnd><VolumeIssueCount>6</VolumeIssueCount></VolumeInfo><Issue IssueType="Regular"><IssueInfo TocLevels="0"><IssueIDStart>2</IssueIDStart><IssueIDEnd>2</IssueIDEnd><IssueArticleCount>11</IssueArticleCount><IssueHistory><CoverDate><Year>2001</Year><Month>5</Month></CoverDate></IssueHistory><IssueCopyright><CopyrightHolderName>Kluwer Academic Publishers</CopyrightHolderName><CopyrightYear>2001</CopyrightYear></IssueCopyright></IssueInfo><Article ID="Art7"><ArticleInfo Language="En" ArticleType="OriginalPaper" NumberingStyle="Unnumbered" TocLevels="0" ContainsESM="No"><ArticleID>336196</ArticleID><ArticleDOI>10.1023/A:1010696604330</ArticleDOI><ArticleSequenceNumber>7</ArticleSequenceNumber><ArticleTitle Language="En">DNA binding mediated by the wheat HMGa protein: a novel instance of selectivity against alternating GC sequence</ArticleTitle><ArticleFirstPage>193</ArticleFirstPage><ArticleLastPage>204</ArticleLastPage><ArticleHistory><RegistrationDate><Year>2004</Year><Month>10</Month><Day>3</Day></RegistrationDate></ArticleHistory><ArticleCopyright><CopyrightHolderName>Kluwer Academic Publishers</CopyrightHolderName><CopyrightYear>2001</CopyrightYear></ArticleCopyright><ArticleGrants Type="Regular"><MetadataGrant Grant="OpenAccess"></MetadataGrant><AbstractGrant Grant="OpenAccess"></AbstractGrant><BodyPDFGrant Grant="Restricted"></BodyPDFGrant><BodyHTMLGrant Grant="Restricted"></BodyHTMLGrant><BibliographyGrant Grant="Restricted"></BibliographyGrant><ESMGrant Grant="Restricted"></ESMGrant></ArticleGrants><ArticleContext><JournalID>11103</JournalID><VolumeIDStart>46</VolumeIDStart><VolumeIDEnd>46</VolumeIDEnd><IssueIDStart>2</IssueIDStart><IssueIDEnd>2</IssueIDEnd></ArticleContext></ArticleInfo><ArticleHeader><AuthorGroup><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Chua</GivenName><FamilyName>Yii Leng</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Pwee</GivenName><FamilyName>Keng Hock</FamilyName></AuthorName></Author><Author AffiliationIDS="Aff2"><AuthorName DisplayOrder="Western"><GivenName>R.</GivenName><GivenName>Manjunatha</GivenName><FamilyName>Kini</FamilyName></AuthorName></Author><Affiliation ID="Aff1"><OrgName>Plant Molecular Biology Laboratory</OrgName><OrgAddress><Country>Singapore</Country></OrgAddress></Affiliation><Affiliation ID="Aff2"><OrgDivision>Department of Biological Sciences</OrgDivision><OrgName>National University of Singapore</OrgName><OrgAddress><Street>Block S1A, 10 Science Drive 4</Street><City>Singapore</City><Postcode>117543</Postcode><Country>Republic of Singapore</Country></OrgAddress></Affiliation></AuthorGroup><Abstract ID="Abs1" Language="En"><Heading>Abstract</Heading><Para>The high-mobility-group (HMG) chromosomal protein wheat HMGa was purified to homogeneity and tested for its binding characteristics to double-stranded DNA. Wheat HMGa was able to bind to P268, an A/T-rich fragment derived from the pea plastocyanin gene promoter, producing a small mobility shift in gel retardation assays where the bound complex was sensitive to addition of proteinase K but resistant to heat treatment of the protein, consistent with the identity of wheat HMGa as a putative HMG-I/Y protein. Gel retardation assays and southwestern hybridization analysis revealed that wheat HMGa could selectively interact with the DNA polynucleotides poly(dA).poly(dT), poly(dAdT).poly(dAdT), and poly(dG).poly(dC), but not with poly(dGdC).poly(dGdC). Surface plasmon resonance analysis determined the kinetic and affinity constants of sensor chip-immobilized wheat HMGa for double-stranded DNA 10-mers, revealing a good affinity of the protein for various dinucleotide combinations, except that of alternating GC sequence. Thus contrary to prior reports of a selectivity of wheat HMGa for A/T-rich DNA, the protein appears to be able to interact with sequences containing guanine and cytosine residues as well, except where G/C residues alternate directly in the primary sequence.</Para></Abstract><KeywordGroup Language="En"><Keyword>A/T-rich</Keyword><Keyword>G/C-rich</Keyword><Keyword>high-mobility-group (HMG) proteins</Keyword><Keyword>surface plasmon resonance analysis</Keyword><Keyword>southwestern hybridization</Keyword><Keyword>wheat HMGa</Keyword></KeywordGroup></ArticleHeader><NoBody></NoBody></Article></Issue></Volume></Journal></Publisher></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>DNA binding mediated by the wheat HMGa protein: a novel instance of selectivity against alternating GC sequence</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>DNA binding mediated by the wheat HMGa protein: a novel instance of selectivity against alternating GC sequence</title></titleInfo><name type="personal"><namePart type="given">Chua</namePart><namePart type="family">Yii Leng</namePart><affiliation>Plant Molecular Biology Laboratory, Singapore</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Pwee</namePart><namePart type="family">Keng Hock</namePart><affiliation>Plant Molecular Biology Laboratory, Singapore</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">R.</namePart><namePart type="given">Manjunatha</namePart><namePart type="family">Kini</namePart><affiliation>Department of Biological Sciences, National University of Singapore, Block S1A, 10 Science Drive 4, 117543, Singapore, Republic of Singapore</affiliation><role><roleTerm type="text">author</roleTerm></role></name><typeOfResource>text</typeOfResource><genre type="research-article" displayLabel="OriginalPaper" authority="ISTEX" authorityURI="https://content-type.data.istex.fr" valueURI="https://content-type.data.istex.fr/ark:/67375/XTP-1JC4F85T-7">research-article</genre><originInfo><publisher>Kluwer Academic Publishers</publisher><place><placeTerm type="text">Dordrecht</placeTerm></place><dateIssued encoding="w3cdtf">2001-05-01</dateIssued><copyrightDate encoding="w3cdtf">2001</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><abstract lang="en">Abstract: The high-mobility-group (HMG) chromosomal protein wheat HMGa was purified to homogeneity and tested for its binding characteristics to double-stranded DNA. Wheat HMGa was able to bind to P268, an A/T-rich fragment derived from the pea plastocyanin gene promoter, producing a small mobility shift in gel retardation assays where the bound complex was sensitive to addition of proteinase K but resistant to heat treatment of the protein, consistent with the identity of wheat HMGa as a putative HMG-I/Y protein. Gel retardation assays and southwestern hybridization analysis revealed that wheat HMGa could selectively interact with the DNA polynucleotides poly(dA).poly(dT), poly(dAdT).poly(dAdT), and poly(dG).poly(dC), but not with poly(dGdC).poly(dGdC). Surface plasmon resonance analysis determined the kinetic and affinity constants of sensor chip-immobilized wheat HMGa for double-stranded DNA 10-mers, revealing a good affinity of the protein for various dinucleotide combinations, except that of alternating GC sequence. Thus contrary to prior reports of a selectivity of wheat HMGa for A/T-rich DNA, the protein appears to be able to interact with sequences containing guanine and cytosine residues as well, except where G/C residues alternate directly in the primary sequence.</abstract><subject lang="en"><topic>A/T-rich</topic><topic>G/C-rich</topic><topic>high-mobility-group (HMG) proteins</topic><topic>surface plasmon resonance analysis</topic><topic>southwestern hybridization</topic><topic>wheat HMGa</topic></subject><relatedItem type="host"><titleInfo><title>Plant Molecular Biology</title><subTitle>An International Journal on Molecular Biology, Molecular Genetics and Biochemistry</subTitle></titleInfo><titleInfo type="abbreviated"><title>Plant Mol Biol</title></titleInfo><genre type="journal" authority="ISTEX" authorityURI="https://publication-type.data.istex.fr" valueURI="https://publication-type.data.istex.fr/ark:/67375/JMC-0GLKJH51-B">journal</genre><originInfo><publisher>Springer</publisher><dateIssued encoding="w3cdtf">2001-05-01</dateIssued><copyrightDate encoding="w3cdtf">2001</copyrightDate></originInfo><subject><genre>Life Sciences</genre><topic>Biochemistry, general</topic><topic>Plant Sciences</topic><topic>Plant Pathology</topic></subject><identifier type="ISSN">0167-4412</identifier><identifier type="eISSN">1573-5028</identifier><identifier type="JournalID">11103</identifier><identifier type="IssueArticleCount">11</identifier><identifier type="VolumeIssueCount">6</identifier><part><date>2001</date><detail type="volume"><number>46</number><caption>vol.</caption></detail><detail type="issue"><number>2</number><caption>no.</caption></detail><extent unit="pages"><start>193</start><end>204</end></extent></part><recordInfo><recordOrigin>Kluwer Academic Publishers, 2001</recordOrigin></recordInfo></relatedItem><identifier type="istex">CEC1471031E22FD0AA4A4F4D4E074363743AE8CF</identifier><identifier type="ark">ark:/67375/VQC-8VRKBZR7-D</identifier><identifier type="DOI">10.1023/A:1010696604330</identifier><identifier type="ArticleID">336196</identifier><identifier type="ArticleID">Art7</identifier><accessCondition type="use and reproduction" contentType="copyright">Kluwer Academic Publishers, 2001</accessCondition><recordInfo><recordContentSource authority="ISTEX" authorityURI="https://loaded-corpus.data.istex.fr" valueURI="https://loaded-corpus.data.istex.fr/ark:/67375/XBH-3XSW68JL-F">springer</recordContentSource><recordOrigin>Kluwer Academic Publishers, 2001</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/VQC-8VRKBZR7-D/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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|texte= DNA binding mediated by the wheat HMGa protein: a novel instance of selectivity against alternating GC sequence
}}
| This area was generated with Dilib version V0.6.33. |  |