The 3-hydroxyacyl-ACP dehydratase of mitochondrial fatty acid synthesis in Trypanosoma brucei

Kaija J. Autio; Jennifer L. Guler; Alexander J. Kastaniotis; Paul T. Englund; J. Kalervo Hiltunen

doi:10.1016/j.febslet.2008.01.051

The 3-hydroxyacyl-ACP dehydratase of mitochondrial fatty acid synthesis in Trypanosoma brucei

Kaija J. Autio, Jennifer L. Guler, Alexander J. Kastaniotis, Paul T. Englund, J. Kalervo Hiltunen

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

18 Scopus citations

Abstract

The trypanosomatid parasite Trypanosoma brucei synthesizes fatty acids in the mitochondrion using the type II fatty acid synthesis (FAS) machinery. When mitochondrial FAS was characterized in T. brucei, all of the enzymatic components were identified based on their homology to yeast mitochondrial FAS enzymes, except for 3-hydroxyacyl-ACP dehydratase. Here we describe the characterization of T. brucei mitochondrial 3-hydroxyacyl-ACP dehydratase (TbHTD2), which was identified by its similarity to the human mitochondrial dehydratase. TbHTD2 can rescue the respiratory deficient phenotype of the yeast knock-out strain and restore the lipoic acid content, is localized in the mitochondrion and exhibits hydratase 2 activity.

Original language	English (US)
Pages (from-to)	729-733
Number of pages	5
Journal	FEBS Letters
Volume	582
Issue number	5
DOIs	https://doi.org/10.1016/j.febslet.2008.01.051
State	Published - Mar 5 2008
Externally published	Yes

Keywords

3-Hydroxyacyl-ACP dehydratase
Fatty acid synthesis
Mitochondria
Trypanosoma brucei

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/j.febslet.2008.01.051

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title = "The 3-hydroxyacyl-ACP dehydratase of mitochondrial fatty acid synthesis in Trypanosoma brucei",

abstract = "The trypanosomatid parasite Trypanosoma brucei synthesizes fatty acids in the mitochondrion using the type II fatty acid synthesis (FAS) machinery. When mitochondrial FAS was characterized in T. brucei, all of the enzymatic components were identified based on their homology to yeast mitochondrial FAS enzymes, except for 3-hydroxyacyl-ACP dehydratase. Here we describe the characterization of T. brucei mitochondrial 3-hydroxyacyl-ACP dehydratase (TbHTD2), which was identified by its similarity to the human mitochondrial dehydratase. TbHTD2 can rescue the respiratory deficient phenotype of the yeast knock-out strain and restore the lipoic acid content, is localized in the mitochondrion and exhibits hydratase 2 activity.",

keywords = "3-Hydroxyacyl-ACP dehydratase, Fatty acid synthesis, Mitochondria, Trypanosoma brucei",

author = "Autio, {Kaija J.} and Guler, {Jennifer L.} and Kastaniotis, {Alexander J.} and Englund, {Paul T.} and Hiltunen, {J. Kalervo}",

note = "Funding Information: This work was supported by Grants from the Academy of Finland, the Sigrid Juselius Foundation, NordForsk under the Nordic Centres of Excellence programme in Food, Nutrition and Health, the Project (070010) “MitoHealth” and NIH (AI 21334). TEV-protease was a kind gift from M.Sc. Viivi Majava.",

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doi = "10.1016/j.febslet.2008.01.051",

language = "English (US)",

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T1 - The 3-hydroxyacyl-ACP dehydratase of mitochondrial fatty acid synthesis in Trypanosoma brucei

AU - Autio, Kaija J.

AU - Guler, Jennifer L.

AU - Kastaniotis, Alexander J.

AU - Englund, Paul T.

AU - Hiltunen, J. Kalervo

N1 - Funding Information: This work was supported by Grants from the Academy of Finland, the Sigrid Juselius Foundation, NordForsk under the Nordic Centres of Excellence programme in Food, Nutrition and Health, the Project (070010) “MitoHealth” and NIH (AI 21334). TEV-protease was a kind gift from M.Sc. Viivi Majava.

PY - 2008/3/5

Y1 - 2008/3/5

N2 - The trypanosomatid parasite Trypanosoma brucei synthesizes fatty acids in the mitochondrion using the type II fatty acid synthesis (FAS) machinery. When mitochondrial FAS was characterized in T. brucei, all of the enzymatic components were identified based on their homology to yeast mitochondrial FAS enzymes, except for 3-hydroxyacyl-ACP dehydratase. Here we describe the characterization of T. brucei mitochondrial 3-hydroxyacyl-ACP dehydratase (TbHTD2), which was identified by its similarity to the human mitochondrial dehydratase. TbHTD2 can rescue the respiratory deficient phenotype of the yeast knock-out strain and restore the lipoic acid content, is localized in the mitochondrion and exhibits hydratase 2 activity.

AB - The trypanosomatid parasite Trypanosoma brucei synthesizes fatty acids in the mitochondrion using the type II fatty acid synthesis (FAS) machinery. When mitochondrial FAS was characterized in T. brucei, all of the enzymatic components were identified based on their homology to yeast mitochondrial FAS enzymes, except for 3-hydroxyacyl-ACP dehydratase. Here we describe the characterization of T. brucei mitochondrial 3-hydroxyacyl-ACP dehydratase (TbHTD2), which was identified by its similarity to the human mitochondrial dehydratase. TbHTD2 can rescue the respiratory deficient phenotype of the yeast knock-out strain and restore the lipoic acid content, is localized in the mitochondrion and exhibits hydratase 2 activity.

KW - 3-Hydroxyacyl-ACP dehydratase

KW - Fatty acid synthesis

KW - Mitochondria

KW - Trypanosoma brucei

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SN - 0014-5793

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JO - FEBS Letters

JF - FEBS Letters

IS - 5

ER -

The 3-hydroxyacyl-ACP dehydratase of mitochondrial fatty acid synthesis in Trypanosoma brucei

Abstract

Keywords

ASJC Scopus subject areas

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