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Ice-binding proteins from the fungus Antarctomyces psychrotrophicus possibly originate from two different bacteria through horizontal gene transfer
| Title: | Ice-binding proteins from the fungus Antarctomyces psychrotrophicus possibly originate from two different bacteria through horizontal gene transfer |
| Authors: | Arai, Tatsuya Browse this author | | Fukami, Daichi Browse this author | | Hoshino, Tamotsu Browse this author | | Kondo, Hidemasa Browse this author →KAKEN DB | | Tsuda, Sakae Browse this author →KAKEN DB |
| Keywords: | ascomycete | | freeze resistance | | horizontal gene transfer | | ice-binding protein | | protein structure |
| Issue Date: | Mar-2019 |
| Publisher: | John Wiley & Sons |
| Journal Title: | FEBS Journal |
| Volume: | 286 |
| Issue: | 5 |
| Start Page: | 946 |
| End Page: | 962 |
| Publisher DOI: | 10.1111/febs.14725 |
| Abstract: | Various microbes, including fungi and bacteria, that live in cold environments produce ice-binding proteins (IBPs) that protect them from freezing. Ascomycota and Basidiomycota are two major phyla of fungi, and Antarctomyces psychrotrophicus is currently designated as the sole ascomycete that produces IBP (AnpIBP). However, its complete amino acid sequence, ice-binding property, and evolutionary history have not yet been clarified. Here, we determined the peptide sequences of three new AnpIBP isoforms by total cDNA analysis and compared them with those of other microbial IBPs. The AnpIBP isoforms and ascomycete-putative IBPs were found to be phylogenetically close to the bacterial ones but far from the basidiomycete ones, which is supported by the higher sequence identities to bacterial IBPs than basidiomycete IBPs, although ascomycetes are phylogenetically distant from bacteria. In addition, two of the isoforms of AnpIBP share low sequence identity and are not close in the phylogenetic tree. It is hence presumable that these two AnpIBP isoforms were independently acquired from different bacteria through horizontal gene transfer (HGT), which implies that ascomycetes and bacteria frequently exchange their IBP genes. The non-colligative freezing-point depression ability of AnpIBP was not very high, whereas it exhibited significant abilities of ice recrystallization inhibition, ice shaping, and cryo-protection against freeze-thaw cycles even at submicromolar concentrations. These results suggest that HGT is crucial for the cold-adaptive evolution of ascomycetes, and their IBPs offer freeze resistance to organisms to enable them to inhabit the icy environments of Antarctica. Databases Nucleotide sequence data are available in the DDBJ database under the accession numbers , , for AnpIBP1a, AnpIBP1b, AnpIBP2, respectively. |
| Rights: | This is the peer reviewed version of the following article: The FEBS Journal, Volume286, Issue5, March 2019, Pages 946-962, which has been published in final form at https://doi.org/10.1111/febs.14725 . This article may be used for non-commercial purposes in accordance with Wiley Terms and Conditions for Use of Self-Archived Versions. |
| Type: | article (author version) |
| URI: | http://hdl.handle.net/2115/76829 |
| Appears in Collections: | 生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 津田 栄
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