EliA facilitates the induction of lipase expression by stearyl alcohol in Ralstonia sp. NT80

Akanuma, G; Ishibashi, H; Miyagawa, T; Yoshizawa, R; Watanabe, S; Shiwa, Y; Yoshikawa, H; Ushio, K; Ishizuka, M

HERO ID

4929315

Reference Type

Journal Article

Year

2013

Language

English

PMID

23173706

HERO ID 4929315
In Press No
Year 2013
Title EliA facilitates the induction of lipase expression by stearyl alcohol in Ralstonia sp. NT80
Authors Akanuma, G; Ishibashi, H; Miyagawa, T; Yoshizawa, R; Watanabe, S; Shiwa, Y; Yoshikawa, H; Ushio, K; Ishizuka, M
Journal FEMS Microbiology Letters
Volume 339
Issue 1
Page Numbers 48-56
Abstract Extracellular lipase activity from Ralstonia sp. NT80 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 Pseudomonas 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 ΔeliA 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.
Doi 10.1111/1574-6968.12055
Pmid 23173706
Wosid WOS:000313721100007
Is Certified Translation No
Dupe Override No
Is Public Yes
Language Text English