@article{5bcd29b0358c11df937d000ea68e967b,
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 = dec,
day = "1",
doi = "10.1042/BJ20050664",
language = "English",
volume = "392",
pages = "299--307",
journal = "Biochemical Journal",
issn = "0264-6021",
publisher = "Portland Press Ltd",
number = "Pt 2",
}