Isolation and characterization of a cDNA from flowers of Cynara cardunculus encoding cyprosin (an aspartic proteinase) and its use to study the organ-specific expression of cyprosin
Identifieur interne : 004426 ( Main/Exploration ); précédent : 004425; suivant : 004427Isolation and characterization of a cDNA from flowers of Cynara cardunculus encoding cyprosin (an aspartic proteinase) and its use to study the organ-specific expression of cyprosin
Auteurs : Maria C. Cordeiro [Portugal] ; Zhong-Tian Xue [Suède] ; Marciej Pietrzak [Suisse] ; M. Salomé Pais [Portugal] ; Peter E. Brodelius [Suède]Source :
- Plant Molecular Biology [ 0167-4412 ] ; 1994-03-01.
English descriptors
- KwdEn :
- Teeft :
- Active site aspartyl residues, Amino, Amino acid sequence, Amino acid sequences, Amino acids, Aspartic, Aspartic proteinase, Aspartic proteinases, Bovine chymosin, Cardunculus, Ccap, Ccap hvap osap, Cdna, Chymosin, Clone, Cynara, Cynara cardunculus, Cyprols, Cyprosin, Cyprosin genes, Cyprosins, Early stages, Encoding, Enzyme, Floral development, Flower buds, High homology, Homology, Human cathepsin, Hvap, Hybridization, Large subunit, Nucleotide, Nucleotide sequence, Osap, Other aspartic proteinases, Plant aspartic proteinases, Plant enzymes, Positive clones, Primary structure, Proc natl acad, Proteinase, Putative, Rhizopuspepsin, Rice aspartic proteinase, Tertiary structures.
Abstract
Abstract: Poly(A)+ RNA isolated from flower buds of Cynara cardunculus has been used to prepare a cDNA library. Screening of the cDNA after expression of cloned DNA with antibodies raised against the large subunit of cyprosin 3 resulted in the isolation of six positive clones. One of these clones (cypro1s; a 1.7 kb Eco RI fragment) codes for cyprosin. The nucleotide sequence contain a 1419 bp open reading frame coding for 473 amino acids (aa) including a putative full-length mature protein (440 aa) and a partial prosequence (33 aa). Cypro1s contains a 162 bp 3′ non-coding region followed by a poly(A) tail. The deduced amino acid sequence shows high homology to other plant aspartic proteinases. The homology to mammalian and microbial aspartic proteinases is somewhat lower. Plant aspartic proteinases contain an insert of around 100 aa. We are modelling where this plant-specific insert will appear in the structure of cyprosin. Using cypro1s as a probe in northern blot analysis, the expression of cyprosin in developing flowers and other tissues has been studied. The signal on the northern blot increased for RNA samples from early (flower buds 6 mm in length) to later stages of floral development (flower buds up to 40 mm in length). In late stages of floral development (open flowers 50 mm in length and styles from such flowers) no hybridization signal was visualized showing that the synthesis of mRNA encoding the cyprosin starts in early stages of floral development and switches off at maturation of the flower. Southern blot analysis of genomic DNA showed 4–5 strong hybridizing bands and several minor bands indicating that the cyprosin genes are organized as a multi-gene family in C. cardunculus.
Url:
DOI: 10.1007/BF00029855
Affiliations:
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Brodelius</name><affiliation wicri:level="1"><country xml:lang="fr">Suède</country><wicri:regionArea>Department of Plant Biochemistry, University of Lund, POB 7007, S-22007, Lund</wicri:regionArea><wicri:noRegion>Lund</wicri:noRegion></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="1994-03-01">1994-03-01</date><biblScope unit="volume">24</biblScope><biblScope unit="issue">5</biblScope><biblScope unit="page" from="733">733</biblScope><biblScope unit="page" to="741">741</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>Cynara cardunculus</term><term>amino acid sequence</term><term>aspartic proteinase</term><term>cDNA sequence</term><term>cyprosin</term><term>flower development</term><term>organ specific expression</term></keywords><keywords scheme="Teeft" xml:lang="en"><term>Active site aspartyl residues</term><term>Amino</term><term>Amino acid sequence</term><term>Amino acid sequences</term><term>Amino acids</term><term>Aspartic</term><term>Aspartic proteinase</term><term>Aspartic proteinases</term><term>Bovine chymosin</term><term>Cardunculus</term><term>Ccap</term><term>Ccap hvap osap</term><term>Cdna</term><term>Chymosin</term><term>Clone</term><term>Cynara</term><term>Cynara cardunculus</term><term>Cyprols</term><term>Cyprosin</term><term>Cyprosin genes</term><term>Cyprosins</term><term>Early stages</term><term>Encoding</term><term>Enzyme</term><term>Floral development</term><term>Flower buds</term><term>High homology</term><term>Homology</term><term>Human cathepsin</term><term>Hvap</term><term>Hybridization</term><term>Large subunit</term><term>Nucleotide</term><term>Nucleotide sequence</term><term>Osap</term><term>Other aspartic proteinases</term><term>Plant aspartic proteinases</term><term>Plant enzymes</term><term>Positive clones</term><term>Primary structure</term><term>Proc natl acad</term><term>Proteinase</term><term>Putative</term><term>Rhizopuspepsin</term><term>Rice aspartic proteinase</term><term>Tertiary structures</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Poly(A)+ RNA isolated from flower buds of Cynara cardunculus has been used to prepare a cDNA library. Screening of the cDNA after expression of cloned DNA with antibodies raised against the large subunit of cyprosin 3 resulted in the isolation of six positive clones. One of these clones (cypro1s; a 1.7 kb Eco RI fragment) codes for cyprosin. The nucleotide sequence contain a 1419 bp open reading frame coding for 473 amino acids (aa) including a putative full-length mature protein (440 aa) and a partial prosequence (33 aa). Cypro1s contains a 162 bp 3′ non-coding region followed by a poly(A) tail. The deduced amino acid sequence shows high homology to other plant aspartic proteinases. The homology to mammalian and microbial aspartic proteinases is somewhat lower. Plant aspartic proteinases contain an insert of around 100 aa. We are modelling where this plant-specific insert will appear in the structure of cyprosin. Using cypro1s as a probe in northern blot analysis, the expression of cyprosin in developing flowers and other tissues has been studied. The signal on the northern blot increased for RNA samples from early (flower buds 6 mm in length) to later stages of floral development (flower buds up to 40 mm in length). In late stages of floral development (open flowers 50 mm in length and styles from such flowers) no hybridization signal was visualized showing that the synthesis of mRNA encoding the cyprosin starts in early stages of floral development and switches off at maturation of the flower. Southern blot analysis of genomic DNA showed 4–5 strong hybridizing bands and several minor bands indicating that the cyprosin genes are organized as a multi-gene family in C. cardunculus.</div></front></TEI><affiliations><list><country><li>Portugal</li><li>Suisse</li><li>Suède</li></country></list><tree><country name="Portugal"><noRegion><name sortKey="Cordeiro, Maria C" sort="Cordeiro, Maria C" uniqKey="Cordeiro M" first="Maria C." last="Cordeiro">Maria C. Cordeiro</name></noRegion><name sortKey="Salome Pais, M" sort="Salome Pais, M" uniqKey="Salome Pais M" first="M." last="Salomé Pais">M. Salomé Pais</name></country><country name="Suède"><noRegion><name sortKey="Xue, Zhong Tian" sort="Xue, Zhong Tian" uniqKey="Xue Z" first="Zhong-Tian" last="Xue">Zhong-Tian Xue</name></noRegion><name sortKey="Brodelius, Peter E" sort="Brodelius, Peter E" uniqKey="Brodelius P" first="Peter E." last="Brodelius">Peter E. Brodelius</name></country><country name="Suisse"><noRegion><name sortKey="Pietrzak, Marciej" sort="Pietrzak, Marciej" uniqKey="Pietrzak M" first="Marciej" last="Pietrzak">Marciej Pietrzak</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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