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Title:
Unusual sequence of group 3 LEA (II) mRNA inducible by dehydration stress in wheat | Plant Molecular Biology
Description:
A cDNA clone, pMA1949, detects two mRNA species in wheat seedling tissue that are late embryogenesis-abundant (LEA) and dehydration stress-inducible. Sequence analysis of the pMA1949 clone shows it to be a 991 bp partial cDNA encoding a polypeptide of 317 amino acids with homology to two group 3 LEA proteins, carrot (DC8) and a soybean protein encoded by pGmPM2 cDNA. Molecular analysis of the deduced protein reveals a 33 kDa acidic and extremely hydrophilic protein with potential amphiphilic ฮฑ-helical regions. In addition, the protein contains eleven similar, contiguous repeats of 11 amino acids, which are separated by 118 amino acids from two additional and unique repeats of 36 residues each at the carboxyl end of the protein. Comparisons of sequences of reported group 3 LEA proteins revealed that there are two types, separable by sequence similarity of the 11 amino acid repeating motifs and by the presence or absence of a certain amino acid stretch at the carboxyl terminus. Based on resuls from these comparisons, we propose a second type of group 3 LEA proteins, called group 3 LEA (II).
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month download article/chapter water-stress wheat roots abscisic acid-responsive genes abscisic acid-inducible mrna water-stress induce proc natl acad cold spring harbor molecular biology agricultural research service late embryogenesis-abundant privacy choices/manage cookies full article pdf walker-simmons rights dehydration-induced proteins washington state university dehydration stress-inducible amino acid sequence plant rna preparation amino acid stretch phenol/sds method wheat seedling tissue dormant wheat seeds angiosperm embryo development walker-simmons mk european economic area eliminating โartifact banding chain termination inhibitors mrna rapidly induced conditions privacy policy plant cell 2 soybean protein encoded single-step method article curry accepting optional cookies sequence analysis programs deduced protein reveals extremely hydrophilic protein ho t-hd barley aleurone layers abscisic acid unusual sequence pma1949 clone shows check access cdna-based comparison instant access aba-responsive gene disease research journal finder publish 6 lea proteins lea proteins
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headline:Unusual sequence of group 3 LEA (II) mRNA inducible by dehydration stress in wheat
description:A cDNA clone, pMA1949, detects two mRNA species in wheat seedling tissue that are late embryogenesis-abundant (LEA) and dehydration stress-inducible. Sequence analysis of the pMA1949 clone shows it to be a 991 bp partial cDNA encoding a polypeptide of 317 amino acids with homology to two group 3 LEA proteins, carrot (DC8) and a soybean protein encoded by pGmPM2 cDNA. Molecular analysis of the deduced protein reveals a 33 kDa acidic and extremely hydrophilic protein with potential amphiphilic ฮฑ-helical regions. In addition, the protein contains eleven similar, contiguous repeats of 11 amino acids, which are separated by 118 amino acids from two additional and unique repeats of 36 residues each at the carboxyl end of the protein. Comparisons of sequences of reported group 3 LEA proteins revealed that there are two types, separable by sequence similarity of the 11 amino acid repeating motifs and by the presence or absence of a certain amino acid stretch at the carboxyl terminus. Based on resuls from these comparisons, we propose a second type of group 3 LEA proteins, called group 3 LEA (II).
datePublished:
dateModified:
pageStart:907
pageEnd:912
sameAs:https://doi.org/10.1007/BF00027121
keywords:
abscisic acid
dehydration
LEA
water stress
wheat
Plant Sciences
Biochemistry
general
Plant Pathology
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name:Jeanne Curry
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name:U.S. Department of Agriculture, Agricultural Research Service, Wheat Genetics, Quality, Physiology and Disease Research, Washington State University, Pullman, USA
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headline:Unusual sequence of group 3 LEA (II) mRNA inducible by dehydration stress in wheat
description:A cDNA clone, pMA1949, detects two mRNA species in wheat seedling tissue that are late embryogenesis-abundant (LEA) and dehydration stress-inducible. Sequence analysis of the pMA1949 clone shows it to be a 991 bp partial cDNA encoding a polypeptide of 317 amino acids with homology to two group 3 LEA proteins, carrot (DC8) and a soybean protein encoded by pGmPM2 cDNA. Molecular analysis of the deduced protein reveals a 33 kDa acidic and extremely hydrophilic protein with potential amphiphilic ฮฑ-helical regions. In addition, the protein contains eleven similar, contiguous repeats of 11 amino acids, which are separated by 118 amino acids from two additional and unique repeats of 36 residues each at the carboxyl end of the protein. Comparisons of sequences of reported group 3 LEA proteins revealed that there are two types, separable by sequence similarity of the 11 amino acid repeating motifs and by the presence or absence of a certain amino acid stretch at the carboxyl terminus. Based on resuls from these comparisons, we propose a second type of group 3 LEA proteins, called group 3 LEA (II).
datePublished:
dateModified:
pageStart:907
pageEnd:912
sameAs:https://doi.org/10.1007/BF00027121
keywords:
abscisic acid
dehydration
LEA
water stress
wheat
Plant Sciences
Biochemistry
general
Plant Pathology
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