Evolution of the acyl-CoA binding protein (ACBP)

Mark Burton, Timothy M Rose, Nils J Faergeman, Jens Knudsen

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

Resumé

Udgivelsesdato: 2005-Dec-1
OriginalsprogEngelsk
TidsskriftBiochemical Journal
Vol/bind392
Udgave nummerPt 2
Sider (fra-til)299-307
Antal sider8
ISSN0264-6021
DOI
StatusUdgivet - 1. dec. 2005

Fingeraftryk

Diazepam Binding Inhibitor
Acyl Coenzyme A
Genes
Esters
Protozoa
Gene transfer
Horizontal Gene Transfer
Gene Duplication
Ceramides
Biosynthesis
Ports and harbors
Fungi
Metabolism
Gene expression
Yeast

Citer dette

Burton, Mark ; Rose, Timothy M ; Faergeman, Nils J ; Knudsen, Jens. / Evolution of the acyl-CoA binding protein (ACBP). I: Biochemical Journal. 2005 ; Bind 392, Nr. Pt 2. s. 299-307.
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title = "Evolution of the acyl-CoA binding protein (ACBP)",
abstract = "Acyl-CoA-binding protein (ACBP) is a 10 kDa protein that binds C12-C22 acyl-CoA esters with high affinity. In vitro and in vivo experiments suggest that it is involved in multiple cellular tasks including modulation of fatty acid biosynthesis, enzyme regulation, regulation of the intracellular acyl-CoA pool size, donation of acyl-CoA esters for beta-oxidation, vesicular trafficking, complex lipid synthesis and gene regulation. In the present study, we delineate the evolutionary history of ACBP to get a complete picture of its evolution and distribution among species. ACBP homologues were identified in all four eukaryotic kingdoms, Animalia, Plantae, Fungi and Protista, and eleven eubacterial species. ACBP homologues were not detected in any other known bacterial species, or in archaea. Nearly all of the ACBP-containing bacteria are pathogenic to plants or animals, suggesting that an ACBP gene could have been acquired from a eukaryotic host by horizontal gene transfer. Many bacterial, fungal and higher eukaryotic species only harbour a single ACBP homologue. However, a number of species, ranging from protozoa to vertebrates, have evolved two to six lineage-specific paralogues through gene duplication and/or retrotransposition events. The ACBP protein is highly conserved across phylums, and the majority of ACBP genes are subjected to strong purifying selection. Experimental evidence indicates that the function of ACBP has been conserved from yeast to humans and that the multiple lineage-specific paralogues have evolved altered functions. The appearance of ACBP very early on in evolution points towards a fundamental role of ACBP in acyl-CoA metabolism, including ceramide synthesis and in signalling.",
keywords = "Acyl Coenzyme A, Amino Acid Sequence, Animals, Bacteria, Carrier Proteins, Conserved Sequence, Evolution, Molecular, Fungi, Humans, Invertebrates, Molecular Sequence Data, Multigene Family, Phylogeny, Plants, Sequence Alignment, Sequence Homology, Amino Acid, Species Specificity",
author = "Mark Burton and Rose, {Timothy M} and Faergeman, {Nils J} and Jens Knudsen",
year = "2005",
month = "12",
day = "1",
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volume = "392",
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Evolution of the acyl-CoA binding protein (ACBP). / Burton, Mark; Rose, Timothy M; Faergeman, Nils J; Knudsen, Jens.

I: Biochemical Journal, Bind 392, Nr. Pt 2, 01.12.2005, s. 299-307.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

TY - JOUR

T1 - Evolution of the acyl-CoA binding protein (ACBP)

AU - Burton, Mark

AU - Rose, Timothy M

AU - Faergeman, Nils J

AU - Knudsen, Jens

PY - 2005/12/1

Y1 - 2005/12/1

N2 - Acyl-CoA-binding protein (ACBP) is a 10 kDa protein that binds C12-C22 acyl-CoA esters with high affinity. In vitro and in vivo experiments suggest that it is involved in multiple cellular tasks including modulation of fatty acid biosynthesis, enzyme regulation, regulation of the intracellular acyl-CoA pool size, donation of acyl-CoA esters for beta-oxidation, vesicular trafficking, complex lipid synthesis and gene regulation. In the present study, we delineate the evolutionary history of ACBP to get a complete picture of its evolution and distribution among species. ACBP homologues were identified in all four eukaryotic kingdoms, Animalia, Plantae, Fungi and Protista, and eleven eubacterial species. ACBP homologues were not detected in any other known bacterial species, or in archaea. Nearly all of the ACBP-containing bacteria are pathogenic to plants or animals, suggesting that an ACBP gene could have been acquired from a eukaryotic host by horizontal gene transfer. Many bacterial, fungal and higher eukaryotic species only harbour a single ACBP homologue. However, a number of species, ranging from protozoa to vertebrates, have evolved two to six lineage-specific paralogues through gene duplication and/or retrotransposition events. The ACBP protein is highly conserved across phylums, and the majority of ACBP genes are subjected to strong purifying selection. Experimental evidence indicates that the function of ACBP has been conserved from yeast to humans and that the multiple lineage-specific paralogues have evolved altered functions. The appearance of ACBP very early on in evolution points towards a fundamental role of ACBP in acyl-CoA metabolism, including ceramide synthesis and in signalling.

AB - Acyl-CoA-binding protein (ACBP) is a 10 kDa protein that binds C12-C22 acyl-CoA esters with high affinity. In vitro and in vivo experiments suggest that it is involved in multiple cellular tasks including modulation of fatty acid biosynthesis, enzyme regulation, regulation of the intracellular acyl-CoA pool size, donation of acyl-CoA esters for beta-oxidation, vesicular trafficking, complex lipid synthesis and gene regulation. In the present study, we delineate the evolutionary history of ACBP to get a complete picture of its evolution and distribution among species. ACBP homologues were identified in all four eukaryotic kingdoms, Animalia, Plantae, Fungi and Protista, and eleven eubacterial species. ACBP homologues were not detected in any other known bacterial species, or in archaea. Nearly all of the ACBP-containing bacteria are pathogenic to plants or animals, suggesting that an ACBP gene could have been acquired from a eukaryotic host by horizontal gene transfer. Many bacterial, fungal and higher eukaryotic species only harbour a single ACBP homologue. However, a number of species, ranging from protozoa to vertebrates, have evolved two to six lineage-specific paralogues through gene duplication and/or retrotransposition events. The ACBP protein is highly conserved across phylums, and the majority of ACBP genes are subjected to strong purifying selection. Experimental evidence indicates that the function of ACBP has been conserved from yeast to humans and that the multiple lineage-specific paralogues have evolved altered functions. The appearance of ACBP very early on in evolution points towards a fundamental role of ACBP in acyl-CoA metabolism, including ceramide synthesis and in signalling.

KW - Acyl Coenzyme A

KW - Amino Acid Sequence

KW - Animals

KW - Bacteria

KW - Carrier Proteins

KW - Conserved Sequence

KW - Evolution, Molecular

KW - Fungi

KW - Humans

KW - Invertebrates

KW - Molecular Sequence Data

KW - Multigene Family

KW - Phylogeny

KW - Plants

KW - Sequence Alignment

KW - Sequence Homology, Amino Acid

KW - Species Specificity

U2 - 10.1042/BJ20050664

DO - 10.1042/BJ20050664

M3 - Journal article

C2 - 16018771

VL - 392

SP - 299

EP - 307

JO - Biochemical Journal

JF - Biochemical Journal

SN - 0264-6021

IS - Pt 2

ER -