cDNA sequences, MALDI-TOF analyses, and molecular modelling of barley PR-5 proteins.
Identifieur interne : 000375 ( Main/Exploration ); précédent : 000374; suivant : 000376cDNA sequences, MALDI-TOF analyses, and molecular modelling of barley PR-5 proteins.
Auteurs : Ernst Reiss [Allemagne] ; Bernhard Schlesier ; Wolfgang BrandtSource :
- Phytochemistry [ 0031-9422 ] ; 2006.
Descripteurs français
- KwdFr :
- ADN complémentaire (composition chimique), ADN complémentaire (génétique), Analyse de séquence d'ADN (MeSH), Données de séquences moléculaires (MeSH), Hordeum (génétique), Isoformes de protéines (composition chimique), Isoformes de protéines (génétique), Modèles moléculaires (MeSH), Protéines végétales (composition chimique), Protéines végétales (génétique), Similitude de séquences d'acides aminés (MeSH), Spectrométrie de masse MALDI (méthodes), Structure secondaire des protéines (MeSH), Structure tertiaire des protéines (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
- composition chimique : ADN complémentaire, Isoformes de protéines, Protéines végétales.
- génétique : ADN complémentaire, Hordeum, Isoformes de protéines, Protéines végétales.
- méthodes : Spectrométrie de masse MALDI.
- Analyse de séquence d'ADN, Données de séquences moléculaires, Modèles moléculaires, Similitude de séquences d'acides aminés, Structure secondaire des protéines, Structure tertiaire des protéines, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), DNA, Complementary (chemistry), DNA, Complementary (genetics), Hordeum (genetics), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Plant Proteins (chemistry), Plant Proteins (genetics), Protein Isoforms (chemistry), Protein Isoforms (genetics), Protein Structure, Secondary (MeSH), Protein Structure, Tertiary (MeSH), Sequence Analysis, DNA (MeSH), Sequence Homology, Amino Acid (MeSH), Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization (methods).
- MESH :
- chemical , chemistry : DNA, Complementary, Plant Proteins, Protein Isoforms.
- chemical , genetics : DNA, Complementary, Plant Proteins, Protein Isoforms.
- genetics : Hordeum.
- methods : Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization.
- Amino Acid Sequence, Models, Molecular, Molecular Sequence Data, Protein Structure, Secondary, Protein Structure, Tertiary, Sequence Analysis, DNA, Sequence Homology, Amino Acid.
Abstract
Barley plants are known to produce various PR-5 proteins. Transcripts encoding eight different barley PR-5 proteins (TLPs 1-8, TLP for thaumatin-like protein) were identified and cloned - seven from infected leaves and one from developing grains. Here, we describe the cDNA sequences of four of these TLP isoforms. Moreover, the TLPs from the infected leaves (TLPs 1, 2, and TLPs 4-8) were subjected to MALDI-TOF mass spectrometric measurements that resulted in protein fragments consistent with their deduced peptide sequences. Multiple sequence alignment analysis revealed that the TLPs in barley fall into two groups: long-chain proteins (TLPs 5-8) having 16 cysteine residues and short-chain proteins (TLPs 1-4) with only 10 cysteine residues. Finally, modelling experiments highlighted the effects of sequence differences between the TLP isoforms in terms of their secondary structures and their molecular electrostatic potentials. We propose that these sequence differences have implications for the target preferences of the different isomers.
DOI: 10.1016/j.phytochem.2006.06.014
PubMed: 16876835
Affiliations:
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Le document en format XML
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sort="Schlesier, Bernhard" uniqKey="Schlesier B" first="Bernhard" last="Schlesier">Bernhard Schlesier</name></author><author><name sortKey="Brandt, Wolfgang" sort="Brandt, Wolfgang" uniqKey="Brandt W" first="Wolfgang" last="Brandt">Wolfgang Brandt</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2006">2006</date><idno type="RBID">pubmed:16876835</idno><idno type="pmid">16876835</idno><idno type="doi">10.1016/j.phytochem.2006.06.014</idno><idno type="wicri:Area/Main/Corpus">000385</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000385</idno><idno type="wicri:Area/Main/Curation">000385</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000385</idno><idno type="wicri:Area/Main/Exploration">000385</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">cDNA sequences, MALDI-TOF analyses, and molecular modelling of barley PR-5 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Transcripts encoding eight different barley PR-5 proteins (TLPs 1-8, TLP for thaumatin-like protein) were identified and cloned - seven from infected leaves and one from developing grains. Here, we describe the cDNA sequences of four of these TLP isoforms. Moreover, the TLPs from the infected leaves (TLPs 1, 2, and TLPs 4-8) were subjected to MALDI-TOF mass spectrometric measurements that resulted in protein fragments consistent with their deduced peptide sequences. Multiple sequence alignment analysis revealed that the TLPs in barley fall into two groups: long-chain proteins (TLPs 5-8) having 16 cysteine residues and short-chain proteins (TLPs 1-4) with only 10 cysteine residues. Finally, modelling experiments highlighted the effects of sequence differences between the TLP isoforms in terms of their secondary structures and their molecular electrostatic potentials. We propose that these sequence differences have implications for the target preferences of the different isomers.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16876835</PMID><DateCompleted><Year>2007</Year><Month>01</Month><Day>08</Day></DateCompleted><DateRevised><Year>2006</Year><Month>08</Month><Day>30</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0031-9422</ISSN><JournalIssue CitedMedium="Print"><Volume>67</Volume><Issue>17</Issue><PubDate><Year>2006</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Phytochemistry</Title><ISOAbbreviation>Phytochemistry</ISOAbbreviation></Journal><ArticleTitle>cDNA sequences, MALDI-TOF analyses, and molecular modelling of barley PR-5 proteins.</ArticleTitle><Pagination><MedlinePgn>1856-64</MedlinePgn></Pagination><Abstract><AbstractText>Barley plants are known to produce various PR-5 proteins. Transcripts encoding eight different barley PR-5 proteins (TLPs 1-8, TLP for thaumatin-like protein) were identified and cloned - seven from infected leaves and one from developing grains. Here, we describe the cDNA sequences of four of these TLP isoforms. Moreover, the TLPs from the infected leaves (TLPs 1, 2, and TLPs 4-8) were subjected to MALDI-TOF mass spectrometric measurements that resulted in protein fragments consistent with their deduced peptide sequences. Multiple sequence alignment analysis revealed that the TLPs in barley fall into two groups: long-chain proteins (TLPs 5-8) having 16 cysteine residues and short-chain proteins (TLPs 1-4) with only 10 cysteine residues. Finally, modelling experiments highlighted the effects of sequence differences between the TLP isoforms in terms of their secondary structures and their molecular electrostatic potentials. 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