Abstract

Adenosine triphosphate-binding cassette transporters (ABC transporters) participate in various plant growth and abiotic stress responses. In the present study, 131 ABC genes in barley were systematically identified using bioinformatics. Based on the classification method of the family in rice, these members were classified into eight subfamilies (ABCA–ABCG, ABCI). The conserved domain, amino acid composition, physicochemical properties, chromosome distribution, and tissue expression of these genes were predicted and analyzed. The results showed that the characteristic motifs of the barley ABC genes were highly conserved and there were great diversities in the homology of the transmembrane domain, the number of exons, amino acid length, and the molecular weight, whereas the span of the isoelectric point was small. Tissue expression profile analysis suggested that ABC genes possess non-tissue specificity. Ultimately, 15 differentially expressed genes exhibited diverse expression responses to stress treatments including drought, cadmium, and salt stress, indicating that the ABCB and ABCG subfamilies function in the response to abiotic stress in barley.

Highlights

  • Named after the binding frame of adenosine triphosphate (ATP), ATP-binding cassette transporters (ABC transporters) are widely found in eukaryotes and prokaryotes [1]

  • A total of 131 ABC transporter genes were identified in barley (Supplementary Table S1)

  • The barley ABC genes were classified according to their sequence similarity with rice ABC genes and were further named HvABCA–HvABCG, HvABCI

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Summary

Introduction

Named after the binding frame of adenosine triphosphate (ATP), ATP-binding cassette transporters (ABC transporters) are widely found in eukaryotes and prokaryotes [1]. A previous study found that ABC transporters, as one of the most widely functional protein superfamilies, are involved in plant physiological processes [2], such as plant hormone transport, nutrient uptake by organisms, stomatal regulation [3], environmental stress responses, and the interaction between plants and microorganisms [4]. In contrast to the NBD domain, ABC proteins contain low homologous hydrophobic transmembrane domains (TMDs), and they typically consist of at least six transmembrane α-helices. The NBD domain provides energy through combining and hydrolyzing ATP, whereas the TMD domain is able to select substrates for transportation across membranes through the energy channel provided by the former [7]. TMDs function as selectors for substrates to translocate membrane proteins through the NBD energy channel. A typical ABC full-size transporter have a core unit of two pore-forming

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