cDNA, amino acid and carbohydrate sequence of barley seed-specific peroxidase BP 1

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cDNA, amino acid and carbohydrate sequence of barley seed-specific peroxidase BP 1. / Johansson, Anette; Rasmussen, Søren K.; Harthill, Jean E.; Welinder, Karen G.

In: Plant Molecular Biology, Vol. 18, No. 6, 01.04.1992, p. 1151-1161.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Johansson, A, Rasmussen, SK, Harthill, JE & Welinder, KG 1992, 'cDNA, amino acid and carbohydrate sequence of barley seed-specific peroxidase BP 1', Plant Molecular Biology, vol. 18, no. 6, pp. 1151-1161. https://doi.org/10.1007/BF00047718

APA

Johansson, A., Rasmussen, S. K., Harthill, J. E., & Welinder, K. G. (1992). cDNA, amino acid and carbohydrate sequence of barley seed-specific peroxidase BP 1. Plant Molecular Biology, 18(6), 1151-1161. https://doi.org/10.1007/BF00047718

Vancouver

Johansson A, Rasmussen SK, Harthill JE, Welinder KG. cDNA, amino acid and carbohydrate sequence of barley seed-specific peroxidase BP 1. Plant Molecular Biology. 1992 Apr 1;18(6):1151-1161. https://doi.org/10.1007/BF00047718

Author

Johansson, Anette ; Rasmussen, Søren K. ; Harthill, Jean E. ; Welinder, Karen G. / cDNA, amino acid and carbohydrate sequence of barley seed-specific peroxidase BP 1. In: Plant Molecular Biology. 1992 ; Vol. 18, No. 6. pp. 1151-1161.

Bibtex

@article{6627162b429147e9b289aeef68f2061f,
title = "cDNA, amino acid and carbohydrate sequence of barley seed-specific peroxidase BP 1",
abstract = "The major peroxidase of barley seed BP 1 was characterized. Previous studies showed a low carbohydrate content, low specific activity and tissue-specific expression, and suggested that this basic peroxidase could be particularly useful in the elucidation of the structure-function relationship and in the study of the biological roles of plant peroxidases (S.K. Rasmussen, K.G. Welinder and J. Hejgaard (1991) Plant Mol Biol 16: 317-327). A cDNA library was prepared from mRNA isolated from seeds 15 days after flowering. Full-length clones were obtained and showed 3′ end length variants, a G+C content of 69{\%} in the translated region, a 90{\%} G or C preference in the wobble position of the codons and a typical signal peptide sequence. N-terminal amino acid sequencing and sequence analysis of tryptic peptides verified 98{\%} of the sequence of the mature BP 1 which contains 309 amino acid residues. BP 1 is the first characterized plant peroxidase which is not blocked by pyroglutamate. BP 1 polymorphism was observed. BP 1 is less than 50{\%} identical to other plant peroxidases which, taken together with its developmentally dependent expression in the endosperm 15-20 days after flowering, suggests a unique biological role of this enzyme. The barley peroxidase is processed at the C-terminus and might be targeted to the vacuole. The single site of glycosylation is located near the C-terminus in the N-glycosylation sequon -Asn-Cys-Ser- in which Cys forms part of a disulphide bridge. The major glycan is a typical plant modified-type structure, Manα1-6(Xylβ1-2)Manβ1-4GlcNAcβ1-4(Fucα1-3)GlcNAc. The BP 1 gene was RFLP-mapped on barley chromosome 3, and we propose Prx5 as the name for this new peroxidase locus.",
keywords = "carboxy-terminal processing, glycosylation, Hordeum vulgare L., Prx locus, RFLP, signal peptide, targeting",
author = "Anette Johansson and Rasmussen, {S{\o}ren K.} and Harthill, {Jean E.} and Welinder, {Karen G.}",
year = "1992",
month = "4",
day = "1",
doi = "10.1007/BF00047718",
language = "English",
volume = "18",
pages = "1151--1161",
journal = "Plant Molecular Biology",
issn = "0167-4412",
publisher = "Springer",
number = "6",

}

RIS

TY - JOUR

T1 - cDNA, amino acid and carbohydrate sequence of barley seed-specific peroxidase BP 1

AU - Johansson, Anette

AU - Rasmussen, Søren K.

AU - Harthill, Jean E.

AU - Welinder, Karen G.

PY - 1992/4/1

Y1 - 1992/4/1

N2 - The major peroxidase of barley seed BP 1 was characterized. Previous studies showed a low carbohydrate content, low specific activity and tissue-specific expression, and suggested that this basic peroxidase could be particularly useful in the elucidation of the structure-function relationship and in the study of the biological roles of plant peroxidases (S.K. Rasmussen, K.G. Welinder and J. Hejgaard (1991) Plant Mol Biol 16: 317-327). A cDNA library was prepared from mRNA isolated from seeds 15 days after flowering. Full-length clones were obtained and showed 3′ end length variants, a G+C content of 69% in the translated region, a 90% G or C preference in the wobble position of the codons and a typical signal peptide sequence. N-terminal amino acid sequencing and sequence analysis of tryptic peptides verified 98% of the sequence of the mature BP 1 which contains 309 amino acid residues. BP 1 is the first characterized plant peroxidase which is not blocked by pyroglutamate. BP 1 polymorphism was observed. BP 1 is less than 50% identical to other plant peroxidases which, taken together with its developmentally dependent expression in the endosperm 15-20 days after flowering, suggests a unique biological role of this enzyme. The barley peroxidase is processed at the C-terminus and might be targeted to the vacuole. The single site of glycosylation is located near the C-terminus in the N-glycosylation sequon -Asn-Cys-Ser- in which Cys forms part of a disulphide bridge. The major glycan is a typical plant modified-type structure, Manα1-6(Xylβ1-2)Manβ1-4GlcNAcβ1-4(Fucα1-3)GlcNAc. The BP 1 gene was RFLP-mapped on barley chromosome 3, and we propose Prx5 as the name for this new peroxidase locus.

AB - The major peroxidase of barley seed BP 1 was characterized. Previous studies showed a low carbohydrate content, low specific activity and tissue-specific expression, and suggested that this basic peroxidase could be particularly useful in the elucidation of the structure-function relationship and in the study of the biological roles of plant peroxidases (S.K. Rasmussen, K.G. Welinder and J. Hejgaard (1991) Plant Mol Biol 16: 317-327). A cDNA library was prepared from mRNA isolated from seeds 15 days after flowering. Full-length clones were obtained and showed 3′ end length variants, a G+C content of 69% in the translated region, a 90% G or C preference in the wobble position of the codons and a typical signal peptide sequence. N-terminal amino acid sequencing and sequence analysis of tryptic peptides verified 98% of the sequence of the mature BP 1 which contains 309 amino acid residues. BP 1 is the first characterized plant peroxidase which is not blocked by pyroglutamate. BP 1 polymorphism was observed. BP 1 is less than 50% identical to other plant peroxidases which, taken together with its developmentally dependent expression in the endosperm 15-20 days after flowering, suggests a unique biological role of this enzyme. The barley peroxidase is processed at the C-terminus and might be targeted to the vacuole. The single site of glycosylation is located near the C-terminus in the N-glycosylation sequon -Asn-Cys-Ser- in which Cys forms part of a disulphide bridge. The major glycan is a typical plant modified-type structure, Manα1-6(Xylβ1-2)Manβ1-4GlcNAcβ1-4(Fucα1-3)GlcNAc. The BP 1 gene was RFLP-mapped on barley chromosome 3, and we propose Prx5 as the name for this new peroxidase locus.

KW - carboxy-terminal processing

KW - glycosylation

KW - Hordeum vulgare L.

KW - Prx locus

KW - RFLP

KW - signal peptide

KW - targeting

UR - http://www.scopus.com/inward/record.url?scp=0026844641&partnerID=8YFLogxK

U2 - 10.1007/BF00047718

DO - 10.1007/BF00047718

M3 - Journal article

C2 - 1350932

AN - SCOPUS:0026844641

VL - 18

SP - 1151

EP - 1161

JO - Plant Molecular Biology

JF - Plant Molecular Biology

SN - 0167-4412

IS - 6

ER -

ID: 204471217