Open AccessEliA facilitates the induction of lipase expression by stearyl alcohol in R alstonia sp. NT 80
Author(s) -
Akanuma Genki,
Ishibashi Hayato,
Miyagawa Takahiro,
Yoshizawa Rie,
Watanabe Satoru,
Shiwa Yu,
Yoshikawa Hirofumi,
Ushio Kazutoshi,
Ishizuka Morio
Publication year - 2013
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/1574-6968.12055
Subject(s) - lipase , biochemistry , triacylglycerol lipase , extracellular , biology , chemistry , enzyme
Extracellular lipase activity from R alstonia sp. NT 80 is induced significantly by fatty alcohols such as stearyl alcohol. We found that when lipase expression was induced by stearyl alcohol, a 14‐kDa protein (designated EliA ) was produced concomitantly and abundantly in the culture supernatant. Cloning and sequence analysis revealed that EliA shared 30% identity with the protein‐like activator protein of P seudomonas aeruginosa , which facilitates oxidation and assimilation of n ‐hexadecane. Inactivation of the eliA gene caused a significant reduction in the level of induction of lipase expression by stearyl alcohol. Furthermore, turbidity that was caused by the presence of emulsified stearyl alcohol, an insoluble material, remained in the culture supernatant of the Δ eli A mutant during the late stationary phase, whereas the culture supernatant of the wild type at 72 h was comparatively clear. In contrast, when lipase expression was induced by polyoxyethylene (20) oleyl ether, a soluble material, inactivation of eliA did not affect the extracellular lipase activity greatly. These results strongly indicate that EliA facilitates the induction of lipase expression, presumably by promoting the recognition and/or incorporation of the induction signal that is attributed to stearyl alcohol.