Abstract

BackgroundLampreys are extant representatives of the jawless vertebrate lineage that diverged from jawed vertebrates around 500 million years ago. Lamprey genomes contain information crucial for understanding the evolution of gene families in vertebrates. The ATP-binding cassette (ABC) gene family is found from prokaryotes to eukaryotes. The recent availability of two lamprey draft genomes from sea lamprey Petromyzon marinus and Japanese lamprey Lethenteron japonicum presents an opportunity to infer early evolutionary events of ABC genes in vertebrates.ResultsWe conducted a genome-wide survey of the ABC gene family in two lamprey draft genomes. A total of 37 ABC transporters were identified and classified into seven subfamilies; namely seven ABCA genes, 10 ABCB genes, 10 ABCC genes, three ABCD genes, one ABCE gene, three ABCF genes, and three ABCG genes. The ABCA subfamily has expanded from three genes in sea squirts, seven and nine in lampreys and zebrafish, to 13 and 16 in human and mouse. Conversely, the multiple copies of ABCB1-, ABCG1-, and ABCG2-like genes found in sea squirts have contracted in the other species examined. ABCB2 and ABCB3 seem to be new additions in gnathostomes (not in sea squirts or lampreys), which coincides with the emergence of the gnathostome-specific adaptive immune system. All the genes in the ABCD, ABCE and ABCF subfamilies were conserved and had undergone limited duplication and loss events. In the sea lamprey transcriptomes, the ABCE and ABCF gene subfamilies were ubiquitously and highly expressed in all tissues while the members in other gene subfamilies were differentially expressed.ConclusionsThirteen more lamprey ABC transporter genes were identified in this study compared with a previous study. By concatenating the same gene sequences from the two lampreys, more full length sequences were obtained, which significantly improved both the assignment of gene names and the phylogenetic trees compared with a previous analysis using partial sequences. The ABC gene subfamilies in chordates have undergone obvious expansion or contraction. The ABCA subfamily showed the highest gene expansion rate during chordate evolution. The evolution of ABC transporters in lampreys requires further evaluation because the present results are based on a draft genome.Electronic supplementary materialThe online version of this article (doi:10.1186/s12864-015-1677-z) contains supplementary material, which is available to authorized users.

Highlights

  • Lampreys are extant representatives of the jawless vertebrate lineage that diverged from jawed vertebrates around 500 million years ago

  • Thirteen more lamprey ATP-binding cassette (ABC) transporter genes were identified in this study compared with a previous study

  • The ABC genes were identified independently in the sea lamprey and Japanese lamprey genomes. These sea lamprey and Japanese lamprey ABC gene sequences have been deposited in GenBank and are presented in the Additional file 2, respectively

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Summary

Introduction

Lampreys are extant representatives of the jawless vertebrate lineage that diverged from jawed vertebrates around 500 million years ago. Lamprey genomes contain information crucial for understanding the evolution of gene families in vertebrates. The ATP-binding cassette (ABC) gene family is found from prokaryotes to eukaryotes. The recent availability of two lamprey draft genomes from sea lamprey Petromyzon marinus and Japanese lamprey Lethenteron japonicum presents an opportunity to infer early evolutionary events of ABC genes in vertebrates. The ATP-binding cassette (ABC) gene family encodes membrane-spanning proteins that transport a wide variety of substrates (e.g., ions, sugars, amino acids, lipids, lipopolysaccharides, peptides, metals, toxic metabolites, and xenobiotics) across cell membranes. ABC transporters are ubiquitous in all organisms from prokaryotes to eukaryotes [1,2,3,4]. Most ABC proteins contain an ATP-binding domain ( known as the nucleotidebinding domain, NBD) and a transmembrane domain (TMD). The NBD binds and hydrolyses ATP, providing energy for substrate transport. The TMD consists of five to six membrane spanning helices that determine substrate specificity [5]

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