Abstract
We have isolated and sequenced a 1400-base-pair cDNA derived from gibberellic acid-treated aleurone cell mRNA. This sequence contains an open reading frame that would code for a protein of 361 amino acids. The carboxyl-terminal two-thirds of the predicted amino acid sequence is closely related to that of the rat lysosomal thiol protease cathepsin H; the initial 143 amino acids may code for a secretory peptide plus a prosegment. The expression of this aleurone thiol protease mRNA is unusual in that, in aleurone cells, its abundance is regulated by the plant hormones gibberellic acid and abscisic acid, but it is also expressed at high levels in leaf and root tissue. This protease may represent the equivalent of a plant lysosomal thiol protease.
MeSH Terms
Amino Acid Sequence
Base Sequence
Cathepsin H
Cathepsins/genetics
Cysteine Endopeptidases
DNA/genetics
Edible Grain/enzymology
Endopeptidases/genetics,isolation & purification
Enzyme Activation/drug effects
Gibberellins/pharmacology
Hordeum/enzymology
Lysosomes/enzymology
Papain/genetics
Plant Proteins/genetics,isolation & purification
RNA, Messenger/genetics
Recombinant Proteins/genetics
Sequence Homology, Nucleic Acid
Chemicals
Gibberellins
Plant Proteins
RNA, Messenger
Recombinant Proteins
DNA
gibberellic acid
Cathepsins
Endopeptidases
Cysteine Endopeptidases
aleurain
actinidain
Cathepsin H
Ctsh protein, rat
Papain
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Rogers J C
Dean D
Heck G R
References (21)
21 references, click to expand
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