A view of plant dehydrins using antibodies specific to the carboxy terminal peptide

Dehydrins are characterized by the consensus KIKEKLPG amino acid sequence found near the carboxy terminus, and usually repeated from one to many times within the protein. A synthetic peptide containing this consensus sequence was used to produce specific antibodies that recognize dehydrins in a wide...

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Veröffentlicht in:Plant molecular biology 1993-10, Vol.23 (2), p.279-286
Hauptverfasser: Close, T.J. (California Univ., Riverside, CA (USA). Dept. of Botany and Plant Sciences), Fenton, R.D, Moonan, F
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container_issue 2
container_start_page 279
container_title Plant molecular biology
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creator Close, T.J. (California Univ., Riverside, CA (USA). Dept. of Botany and Plant Sciences)
Fenton, R.D
Moonan, F
description Dehydrins are characterized by the consensus KIKEKLPG amino acid sequence found near the carboxy terminus, and usually repeated from one to many times within the protein. A synthetic peptide containing this consensus sequence was used to produce specific antibodies that recognize dehydrins in a wide range of plants. This range covered two families of monocots, viz. Gramineae (Hordeum vulgare L., Triticum aestivum L., Zea mays L., Oryza sativa L.) and Liliaceae (Allium sativa L.), and five families of dicots, Malvaceae (Gossypium hirsutum L.), Solanaceae (Lycopersicon esculentum L.), Brassicaceae (Raphanus sativus L.), Fabaceae (Vigna unguiculata L.), and Cucurbitaceae (Cucumis sativus L.). Two families of gymnosperms, Pinaceae (Pinus edulis Engelm.) and Ginkgoaceae (Ginkgo biloba L.), were also included. For several plants in which dehydrin cDNA and genomic clones have previously been characterized, it now appears that the dehydrin family of proteins is larger, and the regulation of dehydrin expression much more complex, than earlier studies have shown.
doi_str_mv 10.1007/BF00029004
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(California Univ., Riverside, CA (USA). Dept. of Botany and Plant Sciences)</creatorcontrib><creatorcontrib>Fenton, R.D</creatorcontrib><creatorcontrib>Moonan, F</creatorcontrib><title>A view of plant dehydrins using antibodies specific to the carboxy terminal peptide</title><title>Plant molecular biology</title><addtitle>Plant Mol Biol</addtitle><description>Dehydrins are characterized by the consensus KIKEKLPG amino acid sequence found near the carboxy terminus, and usually repeated from one to many times within the protein. A synthetic peptide containing this consensus sequence was used to produce specific antibodies that recognize dehydrins in a wide range of plants. This range covered two families of monocots, viz. 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Psychology</topic><topic>GINKGO BILOBA</topic><topic>GOSSYPIUM HIRSUTUM</topic><topic>Hordeum - chemistry</topic><topic>HORDEUM VULGARE</topic><topic>LYCOPERSICON ESCULENTUM</topic><topic>Molecular Sequence Data</topic><topic>NUCLEOTIDE SEQUENCE</topic><topic>ORYZA SATIVA</topic><topic>PEPTIDE</topic><topic>Peptide Fragments - immunology</topic><topic>PEPTIDES</topic><topic>PEPTIDOS</topic><topic>PINUS</topic><topic>Plant physiology and development</topic><topic>Plant Proteins - analysis</topic><topic>Plant Proteins - immunology</topic><topic>Plants - chemistry</topic><topic>PROTEINAS</topic><topic>PROTEINE</topic><topic>PROTEINS</topic><topic>RAPHANUS SATIVUS</topic><topic>SECUENCIA NUCLEICA</topic><topic>SEQUENCE NUCLEIQUE</topic><topic>Species Specificity</topic><topic>STRESS</topic><topic>Tissue Distribution</topic><topic>TRITICUM AESTIVUM</topic><topic>VIGNA UNGUICULATA</topic><topic>ZEA MAYS</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Close, T.J. 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Dept. of Botany and Plant Sciences)</au><au>Fenton, R.D</au><au>Moonan, F</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A view of plant dehydrins using antibodies specific to the carboxy terminal peptide</atitle><jtitle>Plant molecular biology</jtitle><addtitle>Plant Mol Biol</addtitle><date>1993-10-01</date><risdate>1993</risdate><volume>23</volume><issue>2</issue><spage>279</spage><epage>286</epage><pages>279-286</pages><issn>0167-4412</issn><eissn>1573-5028</eissn><coden>PMBIDB</coden><abstract>Dehydrins are characterized by the consensus KIKEKLPG amino acid sequence found near the carboxy terminus, and usually repeated from one to many times within the protein. A synthetic peptide containing this consensus sequence was used to produce specific antibodies that recognize dehydrins in a wide range of plants. This range covered two families of monocots, viz. Gramineae (Hordeum vulgare L., Triticum aestivum L., Zea mays L., Oryza sativa L.) and Liliaceae (Allium sativa L.), and five families of dicots, Malvaceae (Gossypium hirsutum L.), Solanaceae (Lycopersicon esculentum L.), Brassicaceae (Raphanus sativus L.), Fabaceae (Vigna unguiculata L.), and Cucurbitaceae (Cucumis sativus L.). Two families of gymnosperms, Pinaceae (Pinus edulis Engelm.) and Ginkgoaceae (Ginkgo biloba L.), were also included. For several plants in which dehydrin cDNA and genomic clones have previously been characterized, it now appears that the dehydrin family of proteins is larger, and the regulation of dehydrin expression much more complex, than earlier studies have shown.</abstract><cop>Dordrecht</cop><pub>Springer</pub><pmid>7693020</pmid><doi>10.1007/BF00029004</doi><tpages>8</tpages></addata></record>
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subjects ADN
ALLIUM SATIVUM
Amino Acid Sequence
ANTIBODIES
ANTICORPS
ANTICUERPOS
Biological and medical sciences
Cell biochemistry
Cell physiology
Consensus Sequence
CUCUMIS SATIVUS
DNA
Epitopes
ESTRES
Fundamental and applied biological sciences. Psychology
GINKGO BILOBA
GOSSYPIUM HIRSUTUM
Hordeum - chemistry
HORDEUM VULGARE
LYCOPERSICON ESCULENTUM
Molecular Sequence Data
NUCLEOTIDE SEQUENCE
ORYZA SATIVA
PEPTIDE
Peptide Fragments - immunology
PEPTIDES
PEPTIDOS
PINUS
Plant physiology and development
Plant Proteins - analysis
Plant Proteins - immunology
Plants - chemistry
PROTEINAS
PROTEINE
PROTEINS
RAPHANUS SATIVUS
SECUENCIA NUCLEICA
SEQUENCE NUCLEIQUE
Species Specificity
STRESS
Tissue Distribution
TRITICUM AESTIVUM
VIGNA UNGUICULATA
ZEA MAYS
title A view of plant dehydrins using antibodies specific to the carboxy terminal peptide
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