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The ATP‐dependent Lon protease is involved in many physiological processes. In bacteria, Lon regulates pathogenesis and, in yeast, Lon protects mitochondia from oxidative damage. However, little is known about Lon in fungal phytopathogens. MAP1, a homologue of Lon in Magnaporthe oryzae, was recently identified to be important for stress resistance and pathogenesis. Here, we focus on a novel pathogenic pathway mediated by MAP1. Based on an interaction system between rice and a tandem affinity purification (TAP)‐tagged MAP1 complementation strain, we identified 23 novel fungal proteins from infected leaves using a TAP approach with mass spectrometry, and confirmed that 14 of these proteins physically interact with MAP1 in vivo. Among these 14 proteins, 11 candidates, presumably localized to the mitochondria, were biochemically determined to be substrates of MAP1 hydrolysis. Deletion mutants were created and functionally analysed to further confirm the involvement of these proteins in pathogenesis. The results indicated that all mutants showed reduced conidiation and sensitivity to hydrogen peroxide. Appressorial formations were not affected, although conidia from certain mutants were morphologically altered. In addition, virulence was reduced in four mutants, enhanced (with lesions forming earlier) in two mutants and remained unchanged in one mutant. Together with the known virulence‐related proteins alternative oxidase and enoyl‐CoA hydratase, we propose that most of the Lon‐interacting proteins are involved in the pathogenic regulation pathway mediated by MAP1 in M. oryzae. Perturbation of this pathway may represent an effective approach for the inhibition of rice blast disease.

Electroless copper plating process of N, N, N′, N′-tetrakis (2-hydroxypropyl) ethylenediamine (THPED) chelating agent was researched comprehensively. The results indicate that plating rate decreases with the increase of concentration for THPED, CuSO4 · 5H2O and HCHO, pH value and bath temperature. The additive of K4[Fe(CN)6] · 3H2O, 2, 2′-dipyridyl and polyethylene glycol(PEG) decrease plating rate and K4[Fe(CN)6] · 3H2O has a bad effect on deposits quality, but 2, 2′-dipyridyl and PEG make deposits quality improve greatly. Low concentration of 2-mercaptobenzothiozole (2-MBT) increases plating rate and improves deposits quality, but decreases plating rate and worsens deposits quality when 2-MBT reaches 5 mg/L. The optimal conditions of this electroless copper plating process are that the concentration of THPED, HCHO, CuSO4 · 5H2O, PEG, 2, 2′-dipyridyl and 2-MBT are 16.8 g/L, 16.0 mL/L, 13.3 g/L, 0.5 g/L, 5.0 mg/L and 2.0 mg/L, respectively, pH value is 12.75, bath temperature is 30 °C. Plating rate reaches 9.54 µm/h plating for 30 min in the bath. The SEM images demonstrate that the surface of copper film is smooth and the crystal is fine.