Abstract
Bestatin, an inhibitor of some aminopeptidases in plants and animals, is a powerful inducer of defense genes in tomato leaves; these genes are also induced by herbivore attacks, mechanical wounding, systemin, and methyl jasmonate. Unlike wounding and systemin, bestatin does not cause an increase in intracellular jasmonic acid concentrations, and inhibitors of the octadecanoid pathway do not inhibit induction by bestatin. Furthermore, defense genes were induced by bestatin in a mutant tomato line (JL-5) with a defect in the octadecanoid pathway. Bestatin therefore appears to be exerting its effects close to the level of transcriptional control of these genes, where it may be inhibiting a regulatory protease.
MeSH Terms
Aminopeptidases/antagonists & inhibitors
Animals
Base Sequence
Gene Expression/drug effects
Genes, Plant
Leucine/analogs & derivatives,pharmacology
Lycopersicon esculentum/drug effects,genetics,metabolism
Molecular Sequence Data
Mutation
Oligonucleotide Probes
Peptide Biosynthesis
Peptides
Plant Leaves
Plant Proteins/biosynthesis
Protease Inhibitors/metabolism,pharmacology
Transcription, Genetic
Wounds and Injuries
Chemicals
Oligonucleotide Probes
Peptides
Plant Proteins
Protease Inhibitors
systemin
Aminopeptidases
Leucine
ubenimex
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Schaller A
Institute of Biological Chemistry, Washington State University, Pullman 99164-6340, USA.
Bergey D R
Ryan C A
References (26)
26 references, click to expand
-
Octadecanoid Precursors of Jasmonic Acid Activate the Synthesis of Wound-Inducible Proteinase Inhibitors.
Plant Cell. 1992 Feb;4(2):129-134
PMID: 12297644
-
Nucleotide sequence of a cathepsin D inhibitor protein from tomato.
Plant Physiol. 1993 Dec;103(4):1473
PMID: 8290647
-
Leucine aminopeptidase: an inducible component of the defense response in Lycopersicon esculentum (tomato).
Proc Natl Acad Sci U S A. 1993 Nov 1;90(21):9906-10
PMID: 8234334
-
Systemin activates synthesis of wound-inducible tomato leaf polyphenol oxidase via the octadecanoid defense signaling pathway.
Proc Natl Acad Sci U S A. 1995 Jan 17;92(2):407-11
PMID: 7831300
-
NF-kappa B and Rel: participants in a multiform transcriptional regulatory system.
Int Rev Cytol. 1993;143:1-62
PMID: 8449662
-
Inhibition of NF-kappa B by sodium salicylate and aspirin.
Science. 1994 Aug 12;265(5174):956-9
PMID: 8052854
-
Biosynthetic threonine deaminase gene of tomato: isolation, structure, and upregulation in floral organs.
Proc Natl Acad Sci U S A. 1991 Apr 1;88(7):2678-82
PMID: 2011578
-
Activation of NF-kappa B requires proteolysis of the inhibitor I kappa B-alpha: signal-induced phosphorylation of I kappa B-alpha alone does not release active NF-kappa B.
Proc Natl Acad Sci U S A. 1995 Jan 17;92(2):552-6
PMID: 7831327
-
The ubiquitin-mediated proteolytic pathway: mechanisms of recognition of the proteolytic substrate and involvement in the degradation of native cellular proteins.
FASEB J. 1994 Feb;8(2):182-91
PMID: 8119489
-
Identification of a 50-kDa systemin-binding protein in tomato plasma membranes having Kex2p-like properties.
Proc Natl Acad Sci U S A. 1994 Dec 6;91(25):11802-6
PMID: 7991538
-
A wound-inducible potato proteinase inhibitor gene expressed in non-tuber-bearing species is not sucrose inducible.
Plant Physiol. 1992 Sep;100(1):164-9
PMID: 16652941
-
Structure, expression, and antisense inhibition of the systemin precursor gene.
Science. 1992 Mar 20;255(5051):1570-3
PMID: 1549783
-
Wound-induced proteinase inhibitors from tomato leaves. I. The cDNA-deduced primary structure of pre-inhibitor I and its post-translational processing.
J Biol Chem. 1985 Jun 10;260(11):6555-60
PMID: 2987227
-
Quantitative determination of soluble cellular proteins by radial diffusion in agar gels containing antibodies.
Anal Biochem. 1967 Jun;19(3):434-40
PMID: 4963354
-
Leukotriene A4 hydrolase. Inhibition by bestatin and intrinsic aminopeptidase activity establish its functional resemblance to metallohydrolase enzymes.
J Biol Chem. 1991 Jan 25;266(3):1375-8
PMID: 1846352
-
General roles of abscisic and jasmonic acids in gene activation as a result of mechanical wounding.
Plant Cell. 1992 Sep;4(9):1157-70
PMID: 1392612
-
Molecular cloning and amino acid sequence of rat kidney aminopeptidase M: a member of a super family of zinc-metallohydrolases.
Biochem Biophys Res Commun. 1989 May 30;161(1):236-41
PMID: 2567164
-
Physiologic turnover of nuclear factor kappa B by nuclear proteolysis.
J Biol Chem. 1994 Oct 28;269(43):26594-7
PMID: 7929386
-
Defense-related proteins in higher plants.
Annu Rev Biochem. 1990;59:873-907
PMID: 2197993
-
A polypeptide from tomato leaves induces wound-inducible proteinase inhibitor proteins.
Science. 1991 Aug 23;253(5022):895-7
PMID: 17751827
-
Bestatin, an inhibitor of aminopeptidase B, produced by actinomycetes.
J Antibiot (Tokyo). 1976 Jan;29(1):97-9
PMID: 931798
-
Isolation and characterization of the proteinase inhibitor-inducing factor from tomato leaves. Identity and activity of poly- and oligogalacturonide fragments.
J Biol Chem. 1984 Nov 10;259(21):13172-7
PMID: 6490652
-
Biosynthesis of jasmonic Acid by several plant species.
Plant Physiol. 1984 Jun;75(2):458-61
PMID: 16663643
-
Structure-activity of deleted and substituted systemin, an 18-amino acid polypeptide inducer of plant defensive genes.
J Biol Chem. 1993 Jan 5;268(1):212-6
PMID: 8416929
-
Isolation of signaling mutants of tomato (Lycopersicon esculentum).
Mol Gen Genet. 1993 Dec;241(5-6):595-601
PMID: 8264534
-
Proteinase inhibitor synthesis in tomato leaves : induction by chitosan oligomers and chemically modified chitosan and chitin.
Plant Physiol. 1984 Nov;76(3):787-90
PMID: 16663925