Monascus azaphilone pigment biosynthesis employs a dedicated fatty acid synthase for short chain fatty acyl moieties

Bijinu Balakrishnan; Hyun Ju Kim; Jae Won Suh; Chien Chi Chen; Kwang Hyeon Liu; Si Hyung Park; Hyung Jin Kwon

doi:10.1007/s13765-014-4017-0

Monascus azaphilone pigment biosynthesis employs a dedicated fatty acid synthase for short chain fatty acyl moieties

Bijinu Balakrishnan, Hyun Ju Kim, Jae Won Suh, Chien Chi Chen, Kwang Hyeon Liu, Si Hyung Park, Hyung Jin Kwon

Research output: Contribution to journal › Article › peer-review

40 Scopus citations

Abstract

The biosynthetic gene cluster of Monascus azaphilone pigments (MAzPs) encodes a canonical fatty acid synthase, MpFAS2. It is thus proposed that MpFAS2 plays a role in MAzP biosynthesis by supplying short chain (C8 and C10) fatty acyl moieties. Targeted gene inactivation of MpfasB2 in Monascus purpureus generated an F9 mutant, which developed white hyphae that discharged a yellow color on potato dextrose agar. High-performance liquid chromatography analysis demonstrated that F9 was incapable of producing MAzP and accumulated a wide array of chromophoric compounds instead. The main compound found in F9 was monascusone A, a hydrogenated azaphilone lacking a fatty acyl moiety. Gas chromatography analysis of the fatty acid methyl esters indicated that there was no significant difference in the cellular fatty acyl (C16 and C18) contents between WT and F9. The present study demonstrates that the dedicated fatty acid synthase is required to decorate the azaphilone polyketides in MAzP biosynthesis.

Original language	English
Pages (from-to)	191-196
Number of pages	6
Journal	Journal of the Korean Society for Applied Biological Chemistry
Volume	57
Issue number	2
DOIs	https://doi.org/10.1007/s13765-014-4017-0
State	Published - Apr 2014

Keywords

azaphilone pigment biosynthesis
fatty acid synthase
Monascus purpureus polyketide biosynthesis

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title = "Monascus azaphilone pigment biosynthesis employs a dedicated fatty acid synthase for short chain fatty acyl moieties",

abstract = "The biosynthetic gene cluster of Monascus azaphilone pigments (MAzPs) encodes a canonical fatty acid synthase, MpFAS2. It is thus proposed that MpFAS2 plays a role in MAzP biosynthesis by supplying short chain (C8 and C10) fatty acyl moieties. Targeted gene inactivation of MpfasB2 in Monascus purpureus generated an F9 mutant, which developed white hyphae that discharged a yellow color on potato dextrose agar. High-performance liquid chromatography analysis demonstrated that F9 was incapable of producing MAzP and accumulated a wide array of chromophoric compounds instead. The main compound found in F9 was monascusone A, a hydrogenated azaphilone lacking a fatty acyl moiety. Gas chromatography analysis of the fatty acid methyl esters indicated that there was no significant difference in the cellular fatty acyl (C16 and C18) contents between WT and F9. The present study demonstrates that the dedicated fatty acid synthase is required to decorate the azaphilone polyketides in MAzP biosynthesis.",

keywords = "azaphilone pigment biosynthesis, fatty acid synthase, Monascus purpureus polyketide biosynthesis",

author = "Bijinu Balakrishnan and Kim, {Hyun Ju} and Suh, {Jae Won} and Chen, {Chien Chi} and Liu, {Kwang Hyeon} and Park, {Si Hyung} and Kwon, {Hyung Jin}",

year = "2014",

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doi = "10.1007/s13765-014-4017-0",

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AU - Balakrishnan, Bijinu

AU - Kim, Hyun Ju

AU - Suh, Jae Won

AU - Chen, Chien Chi

AU - Liu, Kwang Hyeon

AU - Park, Si Hyung

AU - Kwon, Hyung Jin

PY - 2014/4

Y1 - 2014/4

N2 - The biosynthetic gene cluster of Monascus azaphilone pigments (MAzPs) encodes a canonical fatty acid synthase, MpFAS2. It is thus proposed that MpFAS2 plays a role in MAzP biosynthesis by supplying short chain (C8 and C10) fatty acyl moieties. Targeted gene inactivation of MpfasB2 in Monascus purpureus generated an F9 mutant, which developed white hyphae that discharged a yellow color on potato dextrose agar. High-performance liquid chromatography analysis demonstrated that F9 was incapable of producing MAzP and accumulated a wide array of chromophoric compounds instead. The main compound found in F9 was monascusone A, a hydrogenated azaphilone lacking a fatty acyl moiety. Gas chromatography analysis of the fatty acid methyl esters indicated that there was no significant difference in the cellular fatty acyl (C16 and C18) contents between WT and F9. The present study demonstrates that the dedicated fatty acid synthase is required to decorate the azaphilone polyketides in MAzP biosynthesis.

AB - The biosynthetic gene cluster of Monascus azaphilone pigments (MAzPs) encodes a canonical fatty acid synthase, MpFAS2. It is thus proposed that MpFAS2 plays a role in MAzP biosynthesis by supplying short chain (C8 and C10) fatty acyl moieties. Targeted gene inactivation of MpfasB2 in Monascus purpureus generated an F9 mutant, which developed white hyphae that discharged a yellow color on potato dextrose agar. High-performance liquid chromatography analysis demonstrated that F9 was incapable of producing MAzP and accumulated a wide array of chromophoric compounds instead. The main compound found in F9 was monascusone A, a hydrogenated azaphilone lacking a fatty acyl moiety. Gas chromatography analysis of the fatty acid methyl esters indicated that there was no significant difference in the cellular fatty acyl (C16 and C18) contents between WT and F9. The present study demonstrates that the dedicated fatty acid synthase is required to decorate the azaphilone polyketides in MAzP biosynthesis.

KW - azaphilone pigment biosynthesis

KW - fatty acid synthase

KW - Monascus purpureus polyketide biosynthesis

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Monascus azaphilone pigment biosynthesis employs a dedicated fatty acid synthase for short chain fatty acyl moieties

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Keywords

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