Abstract
UMAMIT proteins have been known as key players in amino acid transport. In Arabidopsis, functions of several UMAMITs have been characterized, but their precise mechanism, evolutionary history and functional divergence remain elusive. In this study, we conducted phylogenetic analysis of the UMAMIT gene family across key species in the evolutionary history of plants, ranging from algae to angiosperms. Our findings indicate that UMAMIT proteins underwent a substantial expansion from algae to angiosperms, accompanied by the stabilization of the EamA (the main domain of UMAMIT) structure. Phylogenetic studies suggest that UMAMITs may have originated from green algae and be divided into four subfamilies. These proteins first diversified in bryophytes and subsequently experienced gene duplication events in seed plants. Subfamily I was potentially associated with amino acid transport in seeds. Regarding subcellular localization, UMAMITs were predominantly localized in the plasma membrane and chloroplasts. However, members from clade 8 in subfamily III exhibited specific localization in the tonoplast. These members may have multiple functions, such as plant disease resistance and root development. Furthermore, our protein structure prediction revealed that the four-helix bundle motif is crucial in controlling the UMAMIT switch for exporting amino acid. We hypothesize that the specific amino acids in the amino acid binding region determine the type of amino acids being transported. Additionally, subfamily II contains genes that are specifically expressed in reproductive organs and roots in angiosperms, suggesting neofunctionalization. Our study highlights the evolutionary complexity of UMAMITs and underscores their crucial role in the adaptation and diversification of seed plants.
Published Version
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