Structure and organization of two divergent α-amylase genes from barley
Identifieur interne : 001877 ( Istex/Corpus ); précédent : 001876; suivant : 001878Structure and organization of two divergent α-amylase genes from barley
Auteurs : Cheryl A. P. Knox ; Burachai Sonthayanon ; G. Ram Chandra ; Subbaratnam MuthukrishnanSource :
- Plant Molecular Biology [ 0167-4412 ] ; 1987-01-01.
English descriptors
- KwdEn :
- Teeft :
- Aamylase genes, Abscisic acid, Active genes, Agarose, Aleurone, Aleurone layers, Amino, Amino acid sequences, Amino acids, Barley, Barley aleurones, Barley chromosomes, Barley genomic library, Biol, Biol chem, Cdna, Cdna clone, Cdna clones, Cdna probes, Chromosome, Clone, Coding region, Coding regions, Endonuclease, Fragment, Gene, Genomic, Genomic clone, Genomic clones, Gibberellic acid, Hybridization, Intron, Leader peptide region, Lower sequence, Mrna, Muthukrishnan, Nucleotide, Nucleotide sequence identity, Nucleotide sequences, Peptide, Plant molec biol, Primer, Primer extension, Primer extension experiments, Proc natl acad, Promoter regions, Protection experiments, Restriction endonucleases, Restriction maps, Restriction sites, Sequence divergence, Sequencing, Sequencing strategies, Size standards, Specific activity, Sundance, Synthetic oligonucleotides, Transcription, Untranslated sequences, Upper sequence.
Abstract
Abstract: We have isolated several α-amylase genomic clones from an Eco RI library of barley DNA in λ-Charon 32. Five of these clones exhibit unique restriction maps and differences in their abilities to hybridize with two previously characterized α-amylase cDNA probes representing two different loci, α-Amy 1 (high pI) and α-Amy 2 (low pI) on barley chromosomes 6 and 1, respectively. Stringent hybridizations indicate that four of the five genomic clones contain α-Amy 1 sequences and one contains α-Amy 2 sequences. The regions containing α-amylase genes from one representative genomic clone of each group have been sub-cloned, mapped and sequenced. S1-nuclease protection experiments indicate that the two α-amylase genes contained in these clones are functional in aleurone tissue. Transcription start sites in these genes were determined by primer extension using specific synthetic oligonucleotide primers. The DNA sequences of the two α-amylase genes, including promoter regions, are divergent, as are the predicted amino acid sequences of the mature proteins and the N-terminal “leader” peptides. The α-Amy 1 gene contains two introns while the α-Amy 2 gene has three introns. In the coding region, each gene shows 7–10% sequence divergence with respect to the previously characterized cDNA clones of the same gene type. Therefore, differences in nucleotide sequences can account for some of the isozyme variations seen between the sub-families of α-amylases and among members of the same subfamily. Although the nucleotide sequences of the promoter regions of α-Amy 1 and α-Amy 2 genes show little homology, both contain pairs of inverted repeat elements which could constitute regulatory sites.
Url:
DOI: 10.1007/BF00017982
Links to Exploration step
ISTEX:9D688A4F16602472499217048C077BEC99864BB6Le document en format XML
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The α-Amy 1 gene contains two introns while the α-Amy 2 gene has three introns. In the coding region, each gene shows 7–10% sequence divergence with respect to the previously characterized cDNA clones of the same gene type. Therefore, differences in nucleotide sequences can account for some of the isozyme variations seen between the sub-families of α-amylases and among members of the same subfamily. 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Ram Chandra</name><affiliations><json:string>Seed Research Laboratory, BARC-West, 20705, Beltsville, MD, USA</json:string></affiliations></json:item><json:item><name>Subbaratnam Muthukrishnan</name><affiliations><json:string>Department of Biochemistry, Kansas State University, 66506, Manhattan, KS, USA</json:string></affiliations></json:item></author><subject><json:item><lang><json:string>eng</json:string></lang><value>α-amylase genes</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>barley</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>DNA sequence</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>genomic clones</value></json:item><json:item><lang><json:string>eng</json:string></lang><value>transcription starts</value></json:item></subject><articleId><json:string>BF00017982</json:string><json:string>Art1</json:string></articleId><arkIstex>ark:/67375/1BB-PHPZ0GKW-Z</arkIstex><language><json:string>eng</json:string></language><originalGenre><json:string>OriginalPaper</json:string></originalGenre><abstract>Abstract: We have isolated several α-amylase genomic clones from an Eco RI library of barley DNA in λ-Charon 32. Five of these clones exhibit unique restriction maps and differences in their abilities to hybridize with two previously characterized α-amylase cDNA probes representing two different loci, α-Amy 1 (high pI) and α-Amy 2 (low pI) on barley chromosomes 6 and 1, respectively. Stringent hybridizations indicate that four of the five genomic clones contain α-Amy 1 sequences and one contains α-Amy 2 sequences. The regions containing α-amylase genes from one representative genomic clone of each group have been sub-cloned, mapped and sequenced. S1-nuclease protection experiments indicate that the two α-amylase genes contained in these clones are functional in aleurone tissue. Transcription start sites in these genes were determined by primer extension using specific synthetic oligonucleotide primers. The DNA sequences of the two α-amylase genes, including promoter regions, are divergent, as are the predicted amino acid sequences of the mature proteins and the N-terminal “leader” peptides. The α-Amy 1 gene contains two introns while the α-Amy 2 gene has three introns. In the coding region, each gene shows 7–10% sequence divergence with respect to the previously characterized cDNA clones of the same gene type. Therefore, differences in nucleotide sequences can account for some of the isozyme variations seen between the sub-families of α-amylases and among members of the same subfamily. 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Five of these clones exhibit unique restriction maps and differences in their abilities to hybridize with two previously characterized α-amylase cDNA probes representing two different loci, α-Amy 1 (high pI) and α-Amy 2 (low pI) on barley chromosomes 6 and 1, respectively. Stringent hybridizations indicate that four of the five genomic clones contain α-Amy 1 sequences and one contains α-Amy 2 sequences. The regions containing α-amylase genes from one representative genomic clone of each group have been sub-cloned, mapped and sequenced. S1-nuclease protection experiments indicate that the two α-amylase genes contained in these clones are functional in aleurone tissue. Transcription start sites in these genes were determined by primer extension using specific synthetic oligonucleotide primers. The DNA sequences of the two α-amylase genes, including promoter regions, are divergent, as are the predicted amino acid sequences of the mature proteins and the N-terminal “leader” peptides. The α-Amy 1 gene contains two introns while the α-Amy 2 gene has three introns. In the coding region, each gene shows 7–10% sequence divergence with respect to the previously characterized cDNA clones of the same gene type. Therefore, differences in nucleotide sequences can account for some of the isozyme variations seen between the sub-families of α-amylases and among members of the same subfamily. Although the nucleotide sequences of the promoter regions of α-Amy 1 and α-Amy 2 genes show little homology, both contain pairs of inverted repeat elements which could constitute regulatory sites.</p></abstract><textClass xml:lang="en"><keywords scheme="keyword"><list><head>Key words</head><item><term>α-amylase genes</term></item><item><term>barley</term></item><item><term>DNA sequence</term></item><item><term>genomic clones</term></item><item><term>transcription starts</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 when="1986-10-17">Created</change><change 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TocLevels="0"><IssueIDStart>1</IssueIDStart><IssueIDEnd>1</IssueIDEnd><IssueArticleCount>7</IssueArticleCount><IssueHistory><CoverDate><DateString>1987</DateString><Year>1987</Year><Month>1</Month></CoverDate></IssueHistory><IssueCopyright><CopyrightHolderName>Martinus Nijhoff Publishers</CopyrightHolderName><CopyrightYear>1987</CopyrightYear></IssueCopyright></IssueInfo><Article ID="Art1"><ArticleInfo Language="En" ArticleType="OriginalPaper" NumberingStyle="Unnumbered" TocLevels="0" ContainsESM="No"><ArticleID>BF00017982</ArticleID><ArticleDOI>10.1007/BF00017982</ArticleDOI><ArticleSequenceNumber>1</ArticleSequenceNumber><ArticleTitle Language="En">Structure and organization of two divergent α-amylase genes from barley</ArticleTitle><ArticleFirstPage>3</ArticleFirstPage><ArticleLastPage>17</ArticleLastPage><ArticleHistory><RegistrationDate><Year>2004</Year><Month>4</Month><Day>14</Day></RegistrationDate><Received><Year>1986</Year><Month>10</Month><Day>17</Day></Received><Revised><Year>1987</Year><Month>3</Month><Day>2</Day></Revised><Accepted><Year>1987</Year><Month>3</Month><Day>3</Day></Accepted></ArticleHistory><ArticleCopyright><CopyrightHolderName>Martinus Nijhoff Publishers</CopyrightHolderName><CopyrightYear>1987</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>9</VolumeIDStart><VolumeIDEnd>9</VolumeIDEnd><IssueIDStart>1</IssueIDStart><IssueIDEnd>1</IssueIDEnd></ArticleContext></ArticleInfo><ArticleHeader><AuthorGroup><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Cheryl</GivenName><GivenName>A.</GivenName><GivenName>P.</GivenName><FamilyName>Knox</FamilyName></AuthorName><Contact><Phone>913-532-6939</Phone></Contact></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Burachai</GivenName><FamilyName>Sonthayanon</FamilyName></AuthorName><Contact><Phone>913-532-6939</Phone></Contact></Author><Author AffiliationIDS="Aff2"><AuthorName DisplayOrder="Western"><GivenName>G.</GivenName><GivenName>Ram</GivenName><FamilyName>Chandra</FamilyName></AuthorName><Contact><Phone>913-532-6939</Phone></Contact></Author><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Subbaratnam</GivenName><FamilyName>Muthukrishnan</FamilyName></AuthorName><Contact><Phone>913-532-6939</Phone></Contact></Author><Affiliation ID="Aff1"><OrgDivision>Department of Biochemistry</OrgDivision><OrgName>Kansas State University</OrgName><OrgAddress><Postcode>66506</Postcode><City>Manhattan</City><State>KS</State><Country>USA</Country></OrgAddress></Affiliation><Affiliation ID="Aff2"><OrgDivision>Seed Research Laboratory</OrgDivision><OrgName>BARC-West</OrgName><OrgAddress><Postcode>20705</Postcode><City>Beltsville</City><State>MD</State><Country>USA</Country></OrgAddress></Affiliation></AuthorGroup><Abstract ID="Abs1" Language="En"><Heading>Abstract</Heading><Para>We have isolated several α-amylase genomic clones from an Eco RI library of barley DNA in λ-Charon 32. Five of these clones exhibit unique restriction maps and differences in their abilities to hybridize with two previously characterized α-amylase cDNA probes representing two different loci, α-Amy 1 (high pI) and α-Amy 2 (low pI) on barley chromosomes 6 and 1, respectively. Stringent hybridizations indicate that four of the five genomic clones contain α-Amy 1 sequences and one contains α-Amy 2 sequences. The regions containing α-amylase genes from one representative genomic clone of each group have been sub-cloned, mapped and sequenced. S1-nuclease protection experiments indicate that the two α-amylase genes contained in these clones are functional in aleurone tissue. Transcription start sites in these genes were determined by primer extension using specific synthetic oligonucleotide primers.</Para><Para>The DNA sequences of the two α-amylase genes, including promoter regions, are divergent, as are the predicted amino acid sequences of the mature proteins and the N-terminal “leader” peptides. The α-Amy 1 gene contains two introns while the α-Amy 2 gene has three introns. In the coding region, each gene shows 7–10% sequence divergence with respect to the previously characterized cDNA clones of the same gene type. Therefore, differences in nucleotide sequences can account for some of the isozyme variations seen between the sub-families of α-amylases and among members of the same subfamily. Although the nucleotide sequences of the promoter regions of α-Amy 1 and α-Amy 2 genes show little homology, both contain pairs of inverted repeat elements which could constitute regulatory sites.</Para></Abstract><KeywordGroup Language="En"><Heading>Key words</Heading><Keyword>α-amylase genes</Keyword><Keyword>barley</Keyword><Keyword>DNA sequence</Keyword><Keyword>genomic clones</Keyword><Keyword>transcription starts</Keyword></KeywordGroup></ArticleHeader><NoBody></NoBody></Article></Issue></Volume></Journal></Publisher></istex:document></istex:metadataXml><mods version="3.6"><titleInfo lang="en"><title>Structure and organization of two divergent α-amylase genes from barley</title></titleInfo><titleInfo type="alternative" contentType="CDATA"><title>Structure and organization of two divergent α-amylase genes from barley</title></titleInfo><name type="personal"><namePart type="given">Cheryl</namePart><namePart type="given">A.</namePart><namePart type="given">P.</namePart><namePart type="family">Knox</namePart><affiliation>Department of Biochemistry, Kansas State University, 66506, Manhattan, KS, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Burachai</namePart><namePart type="family">Sonthayanon</namePart><affiliation>Department of Biochemistry, Kansas State University, 66506, Manhattan, KS, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">G.</namePart><namePart type="given">Ram</namePart><namePart type="family">Chandra</namePart><affiliation>Seed Research Laboratory, BARC-West, 20705, Beltsville, MD, USA</affiliation><role><roleTerm type="text">author</roleTerm></role></name><name type="personal"><namePart type="given">Subbaratnam</namePart><namePart type="family">Muthukrishnan</namePart><affiliation>Department of Biochemistry, Kansas State University, 66506, Manhattan, KS, USA</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><dateCreated encoding="w3cdtf">1986-10-17</dateCreated><dateIssued encoding="w3cdtf">1987-01-01</dateIssued><copyrightDate encoding="w3cdtf">1987</copyrightDate></originInfo><language><languageTerm type="code" authority="rfc3066">en</languageTerm><languageTerm type="code" authority="iso639-2b">eng</languageTerm></language><abstract lang="en">Abstract: We have isolated several α-amylase genomic clones from an Eco RI library of barley DNA in λ-Charon 32. Five of these clones exhibit unique restriction maps and differences in their abilities to hybridize with two previously characterized α-amylase cDNA probes representing two different loci, α-Amy 1 (high pI) and α-Amy 2 (low pI) on barley chromosomes 6 and 1, respectively. Stringent hybridizations indicate that four of the five genomic clones contain α-Amy 1 sequences and one contains α-Amy 2 sequences. The regions containing α-amylase genes from one representative genomic clone of each group have been sub-cloned, mapped and sequenced. S1-nuclease protection experiments indicate that the two α-amylase genes contained in these clones are functional in aleurone tissue. Transcription start sites in these genes were determined by primer extension using specific synthetic oligonucleotide primers. The DNA sequences of the two α-amylase genes, including promoter regions, are divergent, as are the predicted amino acid sequences of the mature proteins and the N-terminal “leader” peptides. The α-Amy 1 gene contains two introns while the α-Amy 2 gene has three introns. In the coding region, each gene shows 7–10% sequence divergence with respect to the previously characterized cDNA clones of the same gene type. Therefore, differences in nucleotide sequences can account for some of the isozyme variations seen between the sub-families of α-amylases and among members of the same subfamily. Although the nucleotide sequences of the promoter regions of α-Amy 1 and α-Amy 2 genes show little homology, both contain pairs of inverted repeat elements which could constitute regulatory sites.</abstract><subject lang="en"><genre>Key words</genre><topic>α-amylase genes</topic><topic>barley</topic><topic>DNA sequence</topic><topic>genomic clones</topic><topic>transcription starts</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">1987-01-01</dateIssued><copyrightDate encoding="w3cdtf">1987</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">7</identifier><identifier type="VolumeIssueCount">6</identifier><part><date>1987</date><detail type="volume"><number>9</number><caption>vol.</caption></detail><detail type="issue"><number>1</number><caption>no.</caption></detail><extent unit="pages"><start>3</start><end>17</end></extent></part><recordInfo><recordOrigin>Martinus Nijhoff Publishers, 1987</recordOrigin></recordInfo></relatedItem><identifier type="istex">9D688A4F16602472499217048C077BEC99864BB6</identifier><identifier type="ark">ark:/67375/1BB-PHPZ0GKW-Z</identifier><identifier type="DOI">10.1007/BF00017982</identifier><identifier type="ArticleID">BF00017982</identifier><identifier type="ArticleID">Art1</identifier><accessCondition type="use and reproduction" contentType="copyright">Martinus Nijhoff Publishers, 1987</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>Martinus Nijhoff Publishers, 1987</recordOrigin></recordInfo></mods><json:item><extension>json</extension><original>false</original><mimetype>application/json</mimetype><uri>https://api.istex.fr/ark:/67375/1BB-PHPZ0GKW-Z/record.json</uri></json:item></metadata><serie></serie></istex></record>Pour manipuler ce document sous Unix (Dilib)
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