WIP1, a wound-inducible gene from maize with homology to Bowman-Birk proteinase inhibitors

Abstract

We have cloned and sequenced a wound-inducible cDNA clone designated WIP1 (for wound-induced protein) from maize coleoptiles. It was isolated by differential screening of a cDNA library prepared from excised maize coleoptile segments. The deduced amino acid sequence predicts a secretory, cysteine-rich protein of 102 residues with a calculated molecular mass of 11 kDa and a typical N-terminal signal sequence. The protein has about 30% identity with various Bowman-Birk type proteinase inhibitors. Most interestingly, it is novel in that it is double-headed with exclusive specificity for chymotrypsin. WIP1 is strongly wound-induced in contrast to other members of the Bowman-Birk proteinase inhibitor family, which occur in seeds and are regulated during development. The response is fast, similar to defence-induced genes, and measurable as early as 30 min after wounding. Induction can also be evoked in the intact coleoptiles and the signal is systematically transmitted in the coleoptile to adjacent regions of the wounded area. Isolation and analysis of the corresponding genomic clone reveals that WIP1 contains an intron of 90 nucleotides.

Maize death acids, 9-lipoxygenase–derived cyclopente(a)nones, display activity as cytotoxic phytoalexins and transcriptional mediators

“…To validate the microarray results and to compare 10-OPEA activity to other meaningful metabolites, we treated plants with either SA, 12-OPDA, JA, 10-OPEA, DA 0 -4:0, or SLB and compared the expression levels of pathogen-and insect-related genes at 3 h using qRT-PCR. Defense marker genes included ZmOPR2, the maize OPR most strongly up-regulated in response to SLB (40); pathogenesis-related 4b (ZmPR4b) and EF-hand Ca 2+ -binding protein (ZmCCD1), genes involved in the promotion of cell death and pathogen-elicited defense responses (41-43); GST 2 (ZmGST2) and hydrolase (ZmHYD), previously shown to be induced by both insect-and pathogen-related treatments (35,44); a stress-inducible oxidoreductase (ZmOXR); and maize cystatin 9 (ZmCC9), wound inducible protein 1 (ZmWIP1), and serine protease inhibitor (ZmSerPIN), that encode PIs inducible by biotic attack (27,45,46). The defense genes ZmPR4b, ZmOPR2, and ZmCCD1 were strongly induced by 10-OPEA and DA 0 -4:0 treatments with expression levels either statistically equivalent to or higher than those of 12-OPDA, JA, and SA ( Fig.…”

Identification of a Maize Locus That Modulates the Hypersensitive Defense Response, Using Mutant-Assisted Gene Identification and Characterization

“…In maize, the induction of four genes, PR1, PR5, PRms, and Wip1, has been associated with the HR defense response (Casacuberta et al 1992;Rohrmeier and Lehle 1993;Morris et al 1998;Simmons et al 2002). We examined their expression in relation to developing Rp1-D21 lesions by RT-PCR.…”

“…In addition, Figures 2 and 3 show that the Rp1-D21 phenotype is associated with the production of superoxide and H 2 O 2 , together with the induction of the genes PR1, PR5, PRms, and WIP1, all hallmarks of a bona fide HR. It should be noted that these genes can also be induced by a defense response not including HR and by various other stresses including wounding (Casacuberta et al 1991(Casacuberta et al , 1992Rohrmeier and Lehle 1993;Morris et al 1998;Dunkle and Levy 2000). Even so, the preponderance of evidence suggests that Rp1-D21 triggers an exaggerated form of the normal maize hypersensitive response.…”

Multiple isoforms of Pisum trypsin inhibitors result from modification of two primary gene products

“…The two active sites may have different biological significance; for example, the trypsin inhibitory site may be more important in protective functions against pest attack [19], whereas the chymotrypsin site may be of greater importance in the prevention of animal tumour development [21]. However, a wound-induced sequence, deduced to be active only against chymotrypsin, has been reported [18], although an inhibitor function has not been shown for this protein.…”