지원사업
학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
커뮤니티
연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
초록· 키워드
오류제보하기
We have isolated a cDNA clone for the antifungal protein, CaAFP, from hot pepper, Capsicum annuum L. Its open reading frame encodes 85 amino acids, including 8 cysteine residues. CaAFP consists of three domains: a signal peptide, a chitin-binding domain, and a C-terminal peptide domain. The deduced amino acid sequence of the chitin-binding domain shows 92% and 85% similarity to the same domain from PnAMPs and hevein, respectively. Southern blot analysis indicated that CaAFP is present as a single copy, while the northern blots revealed that the clone is highly expressed in the leaves and flower buds, but not in the roots. However, wounding treatments and chemicals generally known to induce PR proteins did not stimulate its expression. In situ hybridization also showed that CaAFP is expressed in the parenchyma cells of the floral sepals. As seen in our functional analysis, this clone was expressed in Escherichia coli, and the fusion protein was purified using nickel-affinity column chromatography. This purified AFP fusion protein inhibited spore germination and appressoria formation in several plant pathogenic fungi, including Fusarium oxisporum and Colletotrichum gloeosporioides. Our results suggest CaAFP is an antifungal protein that defends developing seeds against pathogen invasion while also having a specific biological role during floral development.
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