MOLECULAR CHARACTERIZATION OF NIP1, A GENE ENCODING THE 24KDA ELICITOR FROMFUSARIUM OXYSPORUM F.SP. ERYTHROXYLII

Authors: NELSON, AMY - FORMER BPDL; Birkhold, Patricia; Bailey, Bryan

Submitted to: Molecular Plant-Microbe Interactions
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 6/8/1998
Publication Date: N/A
Citation: N/A

Interpretive Summary: In Peru, an epidemic of vascular wilt disease is presently occurring on Erythroxylum coca, caused by the pathogen, Fusarium oxysporum f. sp. erythroxyli. A genomic clone was isolated and characterized that encodes 24 kDa protein produced by F. oxysporum f. sp. erythroxyli. The protein induces necrosis and ethylene production in E. coca and a wide range of dicots. The gene contains a single small intron, and encodes a protein of 253 amino acids. The deduced amino acid sequence is basic and primarily hydrophobic except for an amino terminal hydrophilic domain, which includes a putative signal sequence. Isolation of the gene will allow manipulation of its expression to understand its role in the host-pathogen interaction, and in the induction of necrosis and ethylene production. This information will be useful to scientists to better understand narcotic plant susceptibility/resistance to Fusarium wilt disease.

Technical Abstract: Fusarium oxysporum f. sp. Erythroxyli produces a 24 kDa protein that is secreted into culture filtrates, and that induces necrosis and ethylene production when applied to the host plant, Erythroxylum coca, or to a broad range of dicots. A genomic clone, Nip1, which encodes the necrosis-inducing peptide, NIP1, has been isolated and characterized. The gene contains a single small intron and encodes a protein of 253 amino acids. Like many previously characterized elicitor molecules, the encode protein is basic and primarily hydrophilic, except for an amino-terminal hydrophobic region encompassing a putative signal sequence.