Molecular cloning of a novel pathogen-inducible cDNA encoding a putative acyl-CoA synthetase from Capsicum annuum L.
Identifieur interne : 001155 ( Istex/Corpus ); précédent : 001154; suivant : 001156Molecular cloning of a novel pathogen-inducible cDNA encoding a putative acyl-CoA synthetase from Capsicum annuum L.
Auteurs : Sang Jik Lee ; Mi-Chung Suh ; Shinje Kim ; Jin-Kyung Kwon ; Minwoo Kim ; Kyung-Hee Paek ; Doil Choi ; Byung-Dong KimSource :
- Plant Molecular Biology [ 0167-4412 ] ; 2001-08-01.
English descriptors
- KwdEn :
Abstract
Abstract: By means of differential display, a pool of salicylic acid (SA)-induced mRNAs were identified and subsequently their cDNAs were isolated from a cDNA library prepared from SA-induced leaf tissues of hot pepper. One of these cDNA clones, designated CaSIG4, was 1900 bp and contained an open reading frame encoding 523 amino acids with a calculated molecular mass of 56.3 kDa. The predicted amino acid sequence of CaSIG4 showed high sequence similarity to the AMP-binding protein family of both prokaryotic and eukaryotic acyl-CoA synthetases. CaSIG4 transcripts accumulated rapidly after SA treatment and in response to both incompatible and compatible interactions with Xanthomonas campestris pv. vesicatoria race 1. To investigate the cis-acting elements mediating CaSIG4 expression, the CaSIG4 5′-flanking region was isolated by inverse PCR. Database searches indicated that a potential cis-regulatory element is almost identical to the consensus core sequences ACC(A/T)ACC(A/C) which are conserved among promoters of other phenylpropanoid biosynthetic genes. The subcellular localization of the CaSIG4 protein was studied by using a soluble modified GFP gene fusion delivered into epidermal cells of onion by biolistic bombardment. The CaSIG4-smGFP fusion protein was localized to the plasma membrane. Taken together, CaSIG4 encoding a putative acyl-CoA synthetase could function as a plasma membrane-bound protein with a role in signaling in plant defense.
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DOI: 10.1023/A:1011677028605
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<front><div type="abstract" xml:lang="en">Abstract: By means of differential display, a pool of salicylic acid (SA)-induced mRNAs were identified and subsequently their cDNAs were isolated from a cDNA library prepared from SA-induced leaf tissues of hot pepper. One of these cDNA clones, designated CaSIG4, was 1900 bp and contained an open reading frame encoding 523 amino acids with a calculated molecular mass of 56.3 kDa. The predicted amino acid sequence of CaSIG4 showed high sequence similarity to the AMP-binding protein family of both prokaryotic and eukaryotic acyl-CoA synthetases. CaSIG4 transcripts accumulated rapidly after SA treatment and in response to both incompatible and compatible interactions with Xanthomonas campestris pv. vesicatoria race 1. To investigate the cis-acting elements mediating CaSIG4 expression, the CaSIG4 5′-flanking region was isolated by inverse PCR. Database searches indicated that a potential cis-regulatory element is almost identical to the consensus core sequences ACC(A/T)ACC(A/C) which are conserved among promoters of other phenylpropanoid biosynthetic genes. The subcellular localization of the CaSIG4 protein was studied by using a soluble modified GFP gene fusion delivered into epidermal cells of onion by biolistic bombardment. The CaSIG4-smGFP fusion protein was localized to the plasma membrane. Taken together, CaSIG4 encoding a putative acyl-CoA synthetase could function as a plasma membrane-bound protein with a role in signaling in plant defense.</div>
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<ArticleDOI>10.1023/A:1011677028605</ArticleDOI>
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<ArticleTitle Language="En">Molecular cloning of a novel pathogen-inducible cDNA encoding a putative acyl-CoA synthetase from Capsicum annuum L.</ArticleTitle>
<ArticleFirstPage>661</ArticleFirstPage>
<ArticleLastPage>671</ArticleLastPage>
<ArticleHistory><RegistrationDate><Year>2004</Year>
<Month>10</Month>
<Day>3</Day>
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<VolumeIDStart>46</VolumeIDStart>
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<ArticleHeader><AuthorGroup><Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Sang</GivenName>
<GivenName>Jik</GivenName>
<FamilyName>Lee</FamilyName>
</AuthorName>
</Author>
<Author AffiliationIDS="Aff2"><AuthorName DisplayOrder="Western"><GivenName>Mi-Chung</GivenName>
<FamilyName>Suh</FamilyName>
</AuthorName>
</Author>
<Author AffiliationIDS="Aff3"><AuthorName DisplayOrder="Western"><GivenName>Shinje</GivenName>
<FamilyName>Kim</FamilyName>
</AuthorName>
</Author>
<Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Jin-Kyung</GivenName>
<FamilyName>Kwon</FamilyName>
</AuthorName>
</Author>
<Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Minwoo</GivenName>
<FamilyName>Kim</FamilyName>
</AuthorName>
</Author>
<Author AffiliationIDS="Aff4"><AuthorName DisplayOrder="Western"><GivenName>Kyung-Hee</GivenName>
<FamilyName>Paek</FamilyName>
</AuthorName>
</Author>
<Author AffiliationIDS="Aff3"><AuthorName DisplayOrder="Western"><GivenName>Doil</GivenName>
<FamilyName>Choi</FamilyName>
</AuthorName>
</Author>
<Author AffiliationIDS="Aff1"><AuthorName DisplayOrder="Western"><GivenName>Byung-Dong</GivenName>
<FamilyName>Kim</FamilyName>
</AuthorName>
</Author>
<Affiliation ID="Aff1"><OrgDivision>School of Plant Science</OrgDivision>
<OrgName>College of Agriculture and Life Sciences</OrgName>
<OrgAddress><Country>Korea</Country>
</OrgAddress>
</Affiliation>
<Affiliation ID="Aff2"><OrgDivision>Plant Cell Biotechnology Laboratory</OrgDivision>
<OrgName>Korea Research Institute of Bioscience and Biotechnology</OrgName>
<OrgAddress><City>Taejon</City>
<Postcode>305-600</Postcode>
<Country>fKorea</Country>
</OrgAddress>
</Affiliation>
<Affiliation ID="Aff3"><OrgDivision>Center for Plant Molecular Genetics and Breeding Research</OrgDivision>
<OrgName>Seoul National University</OrgName>
<OrgAddress><Street>103 Seodoon-dong</Street>
<City>Suwon</City>
<Postcode>441-744</Postcode>
<Country>fKorea</Country>
</OrgAddress>
</Affiliation>
<Affiliation ID="Aff4"><OrgDivision>Plant Molecular Biology and Genetics Laboratory, Graduate School of Biotechnology</OrgDivision>
<OrgName>Korea University</OrgName>
<OrgAddress><City>Seoul</City>
<Postcode>136-701</Postcode>
<Country>Korea</Country>
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<Abstract ID="Abs1" Language="En"><Heading>Abstract</Heading>
<Para>By means of differential display, a pool of salicylic acid (SA)-induced mRNAs were identified and subsequently their cDNAs were isolated from a cDNA library prepared from SA-induced leaf tissues of hot pepper. One of these cDNA clones, designated <Emphasis Type="Italic">CaSIG4</Emphasis>
, was 1900 bp and contained an open reading frame encoding 523 amino acids with a calculated molecular mass of 56.3 kDa. The predicted amino acid sequence of <Emphasis Type="Italic">CaSIG4</Emphasis>
showed high sequence similarity to the AMP-binding protein family of both prokaryotic and eukaryotic acyl-CoA synthetases. <Emphasis Type="Italic">CaSIG4</Emphasis>
transcripts accumulated rapidly after SA treatment and in response to both incompatible and compatible interactions with <Emphasis Type="Italic">Xanthomonas campestris</Emphasis>
pv. <Emphasis Type="Italic">vesicatoria</Emphasis>
race 1. To investigate the <Emphasis Type="Italic">cis</Emphasis>
-acting elements mediating <Emphasis Type="Italic">CaSIG4</Emphasis>
expression, the <Emphasis Type="Italic">CaSIG4</Emphasis>
5′-flanking region was isolated by inverse PCR. Database searches indicated that a potential <Emphasis Type="Italic">cis</Emphasis>
-regulatory element is almost identical to the consensus core sequences ACC(A/T)ACC(A/C) which are conserved among promoters of other phenylpropanoid biosynthetic genes. The subcellular localization of the CaSIG4 protein was studied by using a soluble modified GFP gene fusion delivered into epidermal cells of onion by biolistic bombardment. The CaSIG4-smGFP fusion protein was localized to the plasma membrane. Taken together, CaSIG4 encoding a putative acyl-CoA synthetase could function as a plasma membrane-bound protein with a role in signaling in plant defense.</Para>
</Abstract>
<KeywordGroup Language="En"><Keyword>acyl-CoA synthetase</Keyword>
<Keyword>AMP-binding protein</Keyword>
<Keyword><Emphasis Type="Italic">Capsicum annuum</Emphasis>
L.</Keyword>
<Keyword>mRNA differential display</Keyword>
<Keyword>salicylic acid</Keyword>
<Keyword>subcellular localization</Keyword>
</KeywordGroup>
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<name type="personal"><namePart type="given">Sang</namePart>
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<name type="personal"><namePart type="given">Mi-Chung</namePart>
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<name type="personal"><namePart type="given">Shinje</namePart>
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<name type="personal"><namePart type="given">Jin-Kyung</namePart>
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<name type="personal"><namePart type="given">Kyung-Hee</namePart>
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<name type="personal"><namePart type="given">Doil</namePart>
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<abstract lang="en">Abstract: By means of differential display, a pool of salicylic acid (SA)-induced mRNAs were identified and subsequently their cDNAs were isolated from a cDNA library prepared from SA-induced leaf tissues of hot pepper. One of these cDNA clones, designated CaSIG4, was 1900 bp and contained an open reading frame encoding 523 amino acids with a calculated molecular mass of 56.3 kDa. The predicted amino acid sequence of CaSIG4 showed high sequence similarity to the AMP-binding protein family of both prokaryotic and eukaryotic acyl-CoA synthetases. CaSIG4 transcripts accumulated rapidly after SA treatment and in response to both incompatible and compatible interactions with Xanthomonas campestris pv. vesicatoria race 1. To investigate the cis-acting elements mediating CaSIG4 expression, the CaSIG4 5′-flanking region was isolated by inverse PCR. Database searches indicated that a potential cis-regulatory element is almost identical to the consensus core sequences ACC(A/T)ACC(A/C) which are conserved among promoters of other phenylpropanoid biosynthetic genes. The subcellular localization of the CaSIG4 protein was studied by using a soluble modified GFP gene fusion delivered into epidermal cells of onion by biolistic bombardment. The CaSIG4-smGFP fusion protein was localized to the plasma membrane. Taken together, CaSIG4 encoding a putative acyl-CoA synthetase could function as a plasma membrane-bound protein with a role in signaling in plant defense.</abstract>
<subject lang="en"><topic>acyl-CoA synthetase</topic>
<topic>AMP-binding protein</topic>
<topic>Capsicum annuum L.</topic>
<topic>mRNA differential display</topic>
<topic>salicylic acid</topic>
<topic>subcellular localization</topic>
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<relatedItem type="host"><titleInfo><title>Plant Molecular Biology</title>
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<dateIssued encoding="w3cdtf">2001-08-01</dateIssued>
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<subject><genre>Life Sciences</genre>
<topic>Biochemistry, general</topic>
<topic>Plant Sciences</topic>
<topic>Plant Pathology</topic>
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<identifier type="ISSN">0167-4412</identifier>
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