The ACBP gene family in Rhodnius prolixus: Expression, characterization and function of RpACBP-1

David Majerowicz, Hans K Hannibal-Bach, Rodolfo S C Castro, Bruno L Bozaquel-Morais, Michele Alves-Bezerra, Luciano A M Grillo, Claudio A Masuda, Nils J Færgeman, Jens Knudsen, Katia C Gondim

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

Resumé

The acyl-CoA-binding proteins (ACBP) constitute a family of conserved proteins that bind acyl-CoA with high affinity and protect it from hydrolysis. Thus, ACBPs may have essential roles in basal cellular lipid metabolism. The genome of the insect Rhodnius prolixus encodes five ACBP genes similar to those described for other insect species. The qPCR analysis revealed that these genes have characteristic expression profiles in insect organs, suggesting that they have specific roles in insect physiology. Recombinant RpACBP-1 was able to bind acyl-CoA in an in vitro gel-shift assay. Moreover, heterologous RpACBP-1 expression in acb1Δ mutant yeast rescued the multi-lobed vacuole phenotype, indicating that RpACBP-1 acts as a bona fide acyl-CoA-binding protein. RpACBP-1 knockdown using RNAi caused triacylglycerol accumulation in the insect posterior midgut and a reduction in the number of deposited eggs. The amount of stored triacylglycerol was reduced in flight muscle, and the incorporation of fatty acids in cholesteryl esters was increased in the fat body. These results showed that RpACBP-1 participates in several lipid metabolism steps in R. prolixus.

OriginalsprogEngelsk
TidsskriftInsect Biochemistry and Molecular Biology
Vol/bind72
Sider (fra-til)41-52
ISSN0965-1748
DOI
StatusUdgivet - maj 2016

Fingeraftryk

Diazepam Binding Inhibitor
Rhodnius
Rhodnius prolixus
binding proteins
Acyl Coenzyme A
Genes
insects
Triglycerides
Lipid Metabolism
lipid metabolism
genes
Cholesterol Esters
triacylglycerols
Physiology
insect physiology
Yeast
flight muscles
Fat Body
Muscle
cholesteryl esters

Citer dette

Majerowicz, D., Hannibal-Bach, H. K., Castro, R. S. C., Bozaquel-Morais, B. L., Alves-Bezerra, M., Grillo, L. A. M., ... Gondim, K. C. (2016). The ACBP gene family in Rhodnius prolixus: Expression, characterization and function of RpACBP-1. Insect Biochemistry and Molecular Biology, 72, 41-52. https://doi.org/10.1016/j.ibmb.2016.03.002
Majerowicz, David ; Hannibal-Bach, Hans K ; Castro, Rodolfo S C ; Bozaquel-Morais, Bruno L ; Alves-Bezerra, Michele ; Grillo, Luciano A M ; Masuda, Claudio A ; Færgeman, Nils J ; Knudsen, Jens ; Gondim, Katia C. / The ACBP gene family in Rhodnius prolixus : Expression, characterization and function of RpACBP-1. I: Insect Biochemistry and Molecular Biology. 2016 ; Bind 72. s. 41-52.
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title = "The ACBP gene family in Rhodnius prolixus: Expression, characterization and function of RpACBP-1",
abstract = "The acyl-CoA-binding proteins (ACBP) constitute a family of conserved proteins that bind acyl-CoA with high affinity and protect it from hydrolysis. Thus, ACBPs may have essential roles in basal cellular lipid metabolism. The genome of the insect Rhodnius prolixus encodes five ACBP genes similar to those described for other insect species. The qPCR analysis revealed that these genes have characteristic expression profiles in insect organs, suggesting that they have specific roles in insect physiology. Recombinant RpACBP-1 was able to bind acyl-CoA in an in vitro gel-shift assay. Moreover, heterologous RpACBP-1 expression in acb1Δ mutant yeast rescued the multi-lobed vacuole phenotype, indicating that RpACBP-1 acts as a bona fide acyl-CoA-binding protein. RpACBP-1 knockdown using RNAi caused triacylglycerol accumulation in the insect posterior midgut and a reduction in the number of deposited eggs. The amount of stored triacylglycerol was reduced in flight muscle, and the incorporation of fatty acids in cholesteryl esters was increased in the fat body. These results showed that RpACBP-1 participates in several lipid metabolism steps in R. prolixus.",
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doi = "10.1016/j.ibmb.2016.03.002",
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pages = "41--52",
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Majerowicz, D, Hannibal-Bach, HK, Castro, RSC, Bozaquel-Morais, BL, Alves-Bezerra, M, Grillo, LAM, Masuda, CA, Færgeman, NJ, Knudsen, J & Gondim, KC 2016, 'The ACBP gene family in Rhodnius prolixus: Expression, characterization and function of RpACBP-1', Insect Biochemistry and Molecular Biology, bind 72, s. 41-52. https://doi.org/10.1016/j.ibmb.2016.03.002

The ACBP gene family in Rhodnius prolixus : Expression, characterization and function of RpACBP-1. / Majerowicz, David; Hannibal-Bach, Hans K; Castro, Rodolfo S C; Bozaquel-Morais, Bruno L; Alves-Bezerra, Michele; Grillo, Luciano A M; Masuda, Claudio A; Færgeman, Nils J; Knudsen, Jens; Gondim, Katia C.

I: Insect Biochemistry and Molecular Biology, Bind 72, 05.2016, s. 41-52.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

TY - JOUR

T1 - The ACBP gene family in Rhodnius prolixus

T2 - Expression, characterization and function of RpACBP-1

AU - Majerowicz, David

AU - Hannibal-Bach, Hans K

AU - Castro, Rodolfo S C

AU - Bozaquel-Morais, Bruno L

AU - Alves-Bezerra, Michele

AU - Grillo, Luciano A M

AU - Masuda, Claudio A

AU - Færgeman, Nils J

AU - Knudsen, Jens

AU - Gondim, Katia C

N1 - Copyright © 2016 Elsevier Ltd. All rights reserved.

PY - 2016/5

Y1 - 2016/5

N2 - The acyl-CoA-binding proteins (ACBP) constitute a family of conserved proteins that bind acyl-CoA with high affinity and protect it from hydrolysis. Thus, ACBPs may have essential roles in basal cellular lipid metabolism. The genome of the insect Rhodnius prolixus encodes five ACBP genes similar to those described for other insect species. The qPCR analysis revealed that these genes have characteristic expression profiles in insect organs, suggesting that they have specific roles in insect physiology. Recombinant RpACBP-1 was able to bind acyl-CoA in an in vitro gel-shift assay. Moreover, heterologous RpACBP-1 expression in acb1Δ mutant yeast rescued the multi-lobed vacuole phenotype, indicating that RpACBP-1 acts as a bona fide acyl-CoA-binding protein. RpACBP-1 knockdown using RNAi caused triacylglycerol accumulation in the insect posterior midgut and a reduction in the number of deposited eggs. The amount of stored triacylglycerol was reduced in flight muscle, and the incorporation of fatty acids in cholesteryl esters was increased in the fat body. These results showed that RpACBP-1 participates in several lipid metabolism steps in R. prolixus.

AB - The acyl-CoA-binding proteins (ACBP) constitute a family of conserved proteins that bind acyl-CoA with high affinity and protect it from hydrolysis. Thus, ACBPs may have essential roles in basal cellular lipid metabolism. The genome of the insect Rhodnius prolixus encodes five ACBP genes similar to those described for other insect species. The qPCR analysis revealed that these genes have characteristic expression profiles in insect organs, suggesting that they have specific roles in insect physiology. Recombinant RpACBP-1 was able to bind acyl-CoA in an in vitro gel-shift assay. Moreover, heterologous RpACBP-1 expression in acb1Δ mutant yeast rescued the multi-lobed vacuole phenotype, indicating that RpACBP-1 acts as a bona fide acyl-CoA-binding protein. RpACBP-1 knockdown using RNAi caused triacylglycerol accumulation in the insect posterior midgut and a reduction in the number of deposited eggs. The amount of stored triacylglycerol was reduced in flight muscle, and the incorporation of fatty acids in cholesteryl esters was increased in the fat body. These results showed that RpACBP-1 participates in several lipid metabolism steps in R. prolixus.

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1016/j.ibmb.2016.03.002

DO - 10.1016/j.ibmb.2016.03.002

M3 - Journal article

C2 - 27001070

VL - 72

SP - 41

EP - 52

JO - Insect Biochemistry and Molecular Biology

JF - Insect Biochemistry and Molecular Biology

SN - 0965-1748

ER -

Majerowicz D, Hannibal-Bach HK, Castro RSC, Bozaquel-Morais BL, Alves-Bezerra M, Grillo LAM et al. The ACBP gene family in Rhodnius prolixus: Expression, characterization and function of RpACBP-1. Insect Biochemistry and Molecular Biology. 2016 maj;72:41-52. https://doi.org/10.1016/j.ibmb.2016.03.002