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Aspartic proteinase genes in the Brassicaceae Arabidopsis thaliana and Brassica napus

(1997) PLANT MOLECULAR BIOLOGY. 33(1). p.187-192
Author
Organization
Abstract
Active aspartic proteinase is isolated from Brassica napus seeds and the peptide sequence is used to generate primers for PCR. We present here cDNA and genomic clones for aspartic proteinases from the closely related Brassicaceae Arabidopsis thaliana and Brassica napus. The Arabidopsis cDNA represents a single gene, while Brassica has at least 4 genes. Like other plant aspartic proteases, the two Brassicaceae enzymes contain an extra protein domain of about 100 amino acids relative to the mammalian forms. The intron/exon arrangement in the Brassica genomic clone is significantly different from that in mammalian genes. As the proteinase is isolated from seeds, the same tissue where 2S albumins are processed, this implies expression of one of the aspartic proteinase genes there.
Keywords
aspartic proteinase, gene isolation, intron/exon arrangement, protein processing, pulmonary surfactant-associated protein, saposin C, HUMAN CATHEPSIN-D, HUMAN RENIN GENE, STRUCTURAL-ANALYSIS, SEQUENCE-ANALYSIS, IN-VITRO, BARLEY, CDNA, ORGANIZATION, LOCALIZATION, EXPRESSION

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Chicago
D’Hondt, Kathleen, S Stack, S Gutteridge, Joël Vandekerckhove, E Krebbers, and S Gal. 1997. “Aspartic Proteinase Genes in the Brassicaceae Arabidopsis Thaliana and Brassica Napus.” Plant Molecular Biology 33 (1): 187–192.
APA
D’Hondt, K., Stack, S., Gutteridge, S., Vandekerckhove, J., Krebbers, E., & Gal, S. (1997). Aspartic proteinase genes in the Brassicaceae Arabidopsis thaliana and Brassica napus. PLANT MOLECULAR BIOLOGY, 33(1), 187–192.
Vancouver
1.
D’Hondt K, Stack S, Gutteridge S, Vandekerckhove J, Krebbers E, Gal S. Aspartic proteinase genes in the Brassicaceae Arabidopsis thaliana and Brassica napus. PLANT MOLECULAR BIOLOGY. 1997;33(1):187–92.
MLA
D’Hondt, Kathleen, S Stack, S Gutteridge, et al. “Aspartic Proteinase Genes in the Brassicaceae Arabidopsis Thaliana and Brassica Napus.” PLANT MOLECULAR BIOLOGY 33.1 (1997): 187–192. Print.
@article{182119,
  abstract     = {Active aspartic proteinase is isolated from Brassica napus seeds and the peptide sequence is used to generate primers for PCR. We present here cDNA and genomic clones for aspartic proteinases from the closely related Brassicaceae Arabidopsis thaliana and Brassica napus. The Arabidopsis cDNA represents a single gene, while Brassica has at least 4 genes. Like other plant aspartic proteases, the two Brassicaceae enzymes contain an extra protein domain of about 100 amino acids relative to the mammalian forms. The intron/exon arrangement in the Brassica genomic clone is significantly different from that in mammalian genes. As the proteinase is isolated from seeds, the same tissue where 2S albumins are processed, this implies expression of one of the aspartic proteinase genes there.},
  author       = {D'Hondt, Kathleen and Stack, S and Gutteridge, S and Vandekerckhove, Jo{\"e}l and Krebbers, E and Gal, S},
  issn         = {0167-4412},
  journal      = {PLANT MOLECULAR BIOLOGY},
  keyword      = {aspartic proteinase,gene isolation,intron/exon arrangement,protein processing,pulmonary surfactant-associated protein,saposin C,HUMAN CATHEPSIN-D,HUMAN RENIN GENE,STRUCTURAL-ANALYSIS,SEQUENCE-ANALYSIS,IN-VITRO,BARLEY,CDNA,ORGANIZATION,LOCALIZATION,EXPRESSION},
  language     = {eng},
  number       = {1},
  pages        = {187--192},
  title        = {Aspartic proteinase genes in the Brassicaceae Arabidopsis thaliana and Brassica napus},
  url          = {http://dx.doi.org/10.1023/A:1005794917200},
  volume       = {33},
  year         = {1997},
}

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