A thaumatin-like protein from larvae of the beetle Dendroides canadensis enhances the activity of antifreeze proteins.
Identifieur interne : 000399 ( Main/Exploration ); précédent : 000398; suivant : 000400A thaumatin-like protein from larvae of the beetle Dendroides canadensis enhances the activity of antifreeze proteins.
Auteurs : Lei Wang [États-Unis] ; John G. DumanSource :
- Biochemistry [ 0006-2960 ] ; 2006.
Descripteurs français
- KwdFr :
- Alignement de séquences (MeSH), Animaux (MeSH), Coléoptères (enzymologie), Coléoptères (métabolisme), Données de séquences moléculaires (MeSH), Hémolymphe (métabolisme), Isoformes de protéines (métabolisme), Larve (enzymologie), Larve (métabolisme), Protéines antigel (génétique), Protéines antigel (métabolisme), Protéines recombinantes (génétique), Protéines recombinantes (métabolisme), Protéines végétales (métabolisme), Relation dose-effet des médicaments (MeSH), Séquence d'acides aminés (MeSH), Séquence nucléotidique (MeSH), Techniques de double hybride (MeSH).
- MESH :
- enzymologie : Coléoptères, Larve.
- génétique : Protéines antigel, Protéines recombinantes.
- métabolisme : Coléoptères, Hémolymphe, Isoformes de protéines, Larve, Protéines antigel, Protéines recombinantes, Protéines végétales.
- Alignement de séquences, Animaux, Données de séquences moléculaires, Relation dose-effet des médicaments, Séquence d'acides aminés, Séquence nucléotidique, Techniques de double hybride.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Animals (MeSH), Antifreeze Proteins (genetics), Antifreeze Proteins (metabolism), Base Sequence (MeSH), Coleoptera (enzymology), Coleoptera (metabolism), Dose-Response Relationship, Drug (MeSH), Hemolymph (metabolism), Larva (enzymology), Larva (metabolism), Molecular Sequence Data (MeSH), Plant Proteins (metabolism), Protein Isoforms (metabolism), Recombinant Proteins (genetics), Recombinant Proteins (metabolism), Sequence Alignment (MeSH), Two-Hybrid System Techniques (MeSH).
- MESH :
- chemical , genetics : Antifreeze Proteins, Recombinant Proteins.
- chemical , metabolism : Antifreeze Proteins, Plant Proteins, Protein Isoforms, Recombinant Proteins.
- enzymology : Coleoptera, Larva.
- metabolism : Coleoptera, Hemolymph, Larva.
- Amino Acid Sequence, Animals, Base Sequence, Dose-Response Relationship, Drug, Molecular Sequence Data, Sequence Alignment, Two-Hybrid System Techniques.
Abstract
The levels of thermal hysteresis (antifreeze activity) produced by purified antifreeze proteins (DAFPs) from the larvae of the beetle Dendroides canadensis at endogenous concentrations are lower than what are present in the hemolymph of overwintering larvae. Thermal hysteresis activity of DAFPs is dependent not only on AFP concentration but also on the presence of enhancers that may be either proteins (including other hemolymph DAFPs) or low-molecular mass enhancers such as glycerol. The purpose of this study was to identify endogenous protein enhancers using yeast two-hybrid, co-immunoprecipitation, and finally the enhancement of antifreeze activity. Here we show that a thaumatin-like protein from D. canadensis, until recently known only from plants, significantly enhances the thermal hysteresis of DAFP-1 and -2. Glycerol can further this enhancement, presumably by promoting the interaction of the DAFPs and thaumatin-like protein.
DOI: 10.1021/bi051680r
PubMed: 16430224
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Duman</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2006">2006</date><idno type="RBID">pubmed:16430224</idno><idno type="pmid">16430224</idno><idno type="doi">10.1021/bi051680r</idno><idno type="wicri:Area/Main/Corpus">000402</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000402</idno><idno type="wicri:Area/Main/Curation">000402</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000402</idno><idno type="wicri:Area/Main/Exploration">000402</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">A thaumatin-like protein from larvae of the beetle Dendroides canadensis enhances the activity of antifreeze proteins.</title><author><name sortKey="Wang, Lei" sort="Wang, Lei" uniqKey="Wang L" first="Lei" last="Wang">Lei Wang</name><affiliation wicri:level="1"><nlm:affiliation>Department of Biological Sciences, University of Notre Dame, Notre Dame, Indiana 46556, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biological Sciences, University of Notre Dame, Notre Dame, Indiana 46556</wicri:regionArea><wicri:noRegion>Indiana 46556</wicri:noRegion></affiliation></author><author><name sortKey="Duman, John G" sort="Duman, John G" uniqKey="Duman J" first="John G" last="Duman">John G. 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Thermal hysteresis activity of DAFPs is dependent not only on AFP concentration but also on the presence of enhancers that may be either proteins (including other hemolymph DAFPs) or low-molecular mass enhancers such as glycerol. The purpose of this study was to identify endogenous protein enhancers using yeast two-hybrid, co-immunoprecipitation, and finally the enhancement of antifreeze activity. Here we show that a thaumatin-like protein from D. canadensis, until recently known only from plants, significantly enhances the thermal hysteresis of DAFP-1 and -2. Glycerol can further this enhancement, presumably by promoting the interaction of the DAFPs and thaumatin-like protein.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16430224</PMID><DateCompleted><Year>2006</Year><Month>04</Month><Day>14</Day></DateCompleted><DateRevised><Year>2017</Year><Month>11</Month><Day>16</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-2960</ISSN><JournalIssue CitedMedium="Print"><Volume>45</Volume><Issue>4</Issue><PubDate><Year>2006</Year><Month>Jan</Month><Day>31</Day></PubDate></JournalIssue><Title>Biochemistry</Title><ISOAbbreviation>Biochemistry</ISOAbbreviation></Journal><ArticleTitle>A thaumatin-like protein from larvae of the beetle Dendroides canadensis enhances the activity of antifreeze proteins.</ArticleTitle><Pagination><MedlinePgn>1278-84</MedlinePgn></Pagination><Abstract><AbstractText>The levels of thermal hysteresis (antifreeze activity) produced by purified antifreeze proteins (DAFPs) from the larvae of the beetle Dendroides canadensis at endogenous concentrations are lower than what are present in the hemolymph of overwintering larvae. Thermal hysteresis activity of DAFPs is dependent not only on AFP concentration but also on the presence of enhancers that may be either proteins (including other hemolymph DAFPs) or low-molecular mass enhancers such as glycerol. The purpose of this study was to identify endogenous protein enhancers using yeast two-hybrid, co-immunoprecipitation, and finally the enhancement of antifreeze activity. Here we show that a thaumatin-like protein from D. canadensis, until recently known only from plants, significantly enhances the thermal hysteresis of DAFP-1 and -2. 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Duman</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Wang, Lei" sort="Wang, Lei" uniqKey="Wang L" first="Lei" last="Wang">Lei Wang</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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