title: Molecular properties of the class III subfamily of acyl-coenyzme A binding proteins from tung tree (Vernicia fordii).
abstract: Acyl-CoA binding proteins (ACBPs) have been identified in most branches of life, and play various roles in lipid metabolism, among other functions. Plants contain multiple classes of ACBP genes. The most diverse group is the class III proteins. Tung tree (Vernicia fordii) contains two such genes, designated VfACBP3A and VfACBP3B. The two proteins are significantly different in length and sequence. Analysis of tung ACBP3 genes revealed significant evolution, suggesting relatively ancient divergence of the two genes from a common ancestor. Phylogenetic comparisons of multiple plant class III proteins suggest that this group is the most evolutionarily dynamic class of ACBP. Both tung ACBP3 genes are expressed at similar levels in most tissues tested, but ACBP3A is stronger in leaves. Three-dimensional modeling predictions confirmed the presence of the conserved four α-helix bundle acyl-CoA binding (ACB); however, other regions of these proteins likely fold much differently. Acyl-CoA binding assays revealed different affinities for different acyl-CoAs, possibly contradicting the redundancy of function suggested by the gene expression studies. Subcellular targeting of transiently-expressed plant ACBP3 proteins contradicted earlier studies, and suggested that at least some class III ACBPs may be predominantly targeted to endoplasmic reticulum membranes, with little or no targeting to the apoplast.
authors: Southern Regional Research Center, United States Department of Agriculture-Agricultural Research Service, 1100 Robert E. Lee Blvd., New Orleans, LA 70124, USA.
authors: Steven
authors: S
authors: Pastor
authors: Kandan
authors: K
authors: Sethumadhavan
authors: Abul H J
authors: AH
authors: Ullah
authors: Satinder
authors: S
authors: Gidda
authors: Heping
authors: H
authors: Cao
authors: Catherine
authors: C
authors: Mason
authors: Dorselyn
authors: D
authors: Chapital
authors: Brian
authors: B
authors: Scheffler
authors: Robert
authors: R
authors: Mullen
authors: John
authors: J
authors: Dyer
authors: Jay
authors: J
authors: Shockey
mesh_terms: D000214:Acyl Coenzyme A / Q000378:metabolism; D031284:Aleurites / Q000201:enzymology* / Q000235:genetics; D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000201:enzymology / Q000235:genetics; D001483:Base Sequence; D018076:DNA, Complementary / Q000235:genetics; D026261:Diazepam Binding Inhibitor / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D019143:Evolution, Molecular; D035264:Flowers / Q000201:enzymology / Q000235:genetics; D015870:Gene Expression; D018506:Gene Expression Regulation, Plant; D008042:Linolenic Acids / Q000032:analysis; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010802:Phylogeny; D018515:Plant Leaves / Q000201:enzymology / Q000235:genetics; D010940:Plant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D030821:Plants, Genetically Modified; D017434:Protein Structure, Tertiary; D011993:Recombinant Fusion Proteins; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA; D014026:Nicotiana / Q000166:cytology / Q000201:enzymology / Q000235:genetics; D014197:Trees
chemical_list: D000214:Acyl Coenzyme A; D018076:DNA, Complementary; D026261:Diazepam Binding Inhibitor; D008042:Linolenic Acids; D010940:Plant Proteins; D011993:Recombinant Fusion Proteins; C004934:eleostearic acid