Disease relevance of ARPI

• This suggests that the ethylene-responsive proteinase inhibitor does not react with chymotrypsin, as does proteinase inhibitor I, but that it reacts with proteolytic enzymes that cleave at glutamic residues, such as the Staphylococcus aureus V8 proteinase, for which no inhibitors are known [1].

High impact information on ARPI

• A gene that encodes systemin, a mobile 18-amino acid polypeptide inducer of proteinase inhibitor synthesis in tomato and potato leaves, has been isolated from tomato, Lycopersicon esculentum [2].
• This phenotype contrasts with that of untransformed plants, which produce proteinase inhibitor proteins in leaves only in response to wounding or chemical inducers [3].
• Finally, isolation and analysis of a genomic clone reveals that the ethylene-responsive proteinase inhibitor gene is tightly linked to another, yet unidentified, coordinately expressed gene [1].
• Ethylene-regulated expression of a tomato fruit ripening gene encoding a proteinase inhibitor I with a glutamic residue at the reactive site [1].
• DNA sequence analysis of a full-length cDNA clone indicates that the ethylene-responsive gene is distantly related to the tomato proteinase inhibitor I gene, having 53% sequence identity [1].

Biological context of ARPI

• Subsequent sequence analysis indicated that only one copy of the 9-bp direct repeat (target site) was present, suggesting that transposition of the element into the ARPI gene occurred after the divergence of the red-fruited and green-fruited Lycopersicon species [4].
• DNA sequence analysis indicates that one of the ethylene-inducible genes is related to a gene encoding wound-inducible proteinase inhibitor I. We have measured ethylene production during fruit development and detect low basal levels in unripe fruit and much higher levels in ripening fruit [5].
• The predicted amino acid sequence reveals 47% and 45% sequence identity with the tomato and potato proteinase inhibitor I polypeptides, respectively [1].
• A gene coding for proteinase inhibitor I, whose expression is induced in tomato leaves (Lycopersicon esculentum L. var. Bonny Best) in response to wounding or insect attacks, was isolated from a genomic library and characterized [6].
• The inhibition of wound-inducible H(2)O(2) generation and proteinase inhibitor gene expression by NO was not due to an increase in salicylic acid, which is known to inhibit the octadecanoid pathway [7].

Anatomical context of ARPI

• A 90-kDa protein that co-fractionated with thylakoids was induced along with the increase in competence for PPO import, and was identified as the proteinase-inhibitor multicystatin [8].

Associations of ARPI with chemical compounds

• Induction of a proteinase inhibitor II-class gene by auxin in tomato roots [9].
• On day four, proteinase inhibitor activity and particularly transcript levels of salicylate-regulated genes were still maintained [10].
• Decreased resistance of def-1 plants was correlated with reduced JA accumulation and expression of defensive proteinase inhibitor (PI) genes, which were induced in mite-damaged wild-type leaves [11].
• Proteinase inhibitor I expression was repressed by ethylene and induced by 1-methylcyclopropene [12].
• However, H(2)O(2) generated by glucose oxidase and glucose was not blocked by NO, nor was H(2)O(2)-induced proteinase inhibitor synthesis [7].

Regulatory relationships of ARPI

• Tomato plants transformed with an antisense prosystemin complementary DNA exhibited greatly suppressed systemic wound induction of proteinase Inhibitor I and II synthesis in leaves [2].

Other interactions of ARPI

• A segment of DNA 5' to the transcribed region of an auxin-regulated gene, ARPI, from Lycopersicon esculentum Mill. cv. VFN8 contains a sequence with the structural characteristics of a transposable element [4].
• These results suggest that a prosystemin independent- but jasmonic acid-dependent pathway is utilized for proteinase inhibitor accumulation in response to salt stress [13].
• The mutants are deficient in the induction of both proteinase Inhibitor I and proteinase Inhibitor II but can be induced to respond at near wild-type levels by methyl jasmonate, a known elicitor of inhibitor production in tomato [14].

Analytical, diagnostic and therapeutic context of ARPI

• Polymerase chain reaction and Southern analyses revealed that some red-fruited accessions and L. chmielewskii lacked Lyt1 5' to the transcribed region of ARPI [4].
• It has been shown that tomato (Lycopersicon esculentum) plants respond to flame wounding and electrical stimulation by a rapid (15 min) and systemic up-regulation of proteinase inhibitor (pin) genes [15].
• A protein proteinase inhibitor was purified from a seed extract of amaranth (Amaranthus hypochondriacus) by precipitation with (NH4)2SO4, gel-filtration chromatography, ion-exchange chromatography, and reverse-phase high-performance liquid chromatography [16].
• Southern blot analysis was used to study the structural diversity of the aspartic proteinase inhibitor gene family in several species of the Solanaceae [17].

References