An ice‐binding and tandem beta‐sandwich domain‐containing protein in <i>Shewanella frigidimarina</i> is a potential new type of ice adhesin

Vance, Tyler D. R.; Graham, Laurie A.; Davies, Peter L.

doi:10.1111/febs.14424

Cited by 44 publications

(62 citation statements)

References 66 publications

(143 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Thus, this isoform may exist in the intracellular space or on the cell surface. Recently, several reports have shown the existence of such non‐secreted IBPs .…”

Section: Discussionmentioning

confidence: 99%

“…The extension of the N‐ or C‐terminal sequence has sometimes been observed in several IBPs, suggesting that these regions are mostly variable and not conserved. Although their functions have hardly been clarified, several reports have suggested that such additional sequences are responsible for dimerization or anchoring of the protein to the cell surface . The additional C‐terminal sequences of AnpIBP1a and 1b have electrically opposite features (Fig.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Ice‐binding proteins from the fungus Antarctomyces psychrotrophicus possibly originate from two different bacteria through horizontal gene transfer

et al. 2018

View full text Add to dashboard Cite

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.

show abstract

“…Thus, this isoform may exist in the intracellular space or on the cell surface. Recently, several reports have shown the existence of such non‐secreted IBPs .…”

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Ice‐binding proteins from the fungus Antarctomyces psychrotrophicus possibly originate from two different bacteria through horizontal gene transfer

et al. 2018

View full text Add to dashboard Cite

show abstract

“…Other DUF3494‐containing proteins were also found in yeasts, algae, fungi and even archaea from regions that experience cold temperatures. In the last decade, increasing numbers of proteins containing the DUF3494 were demonstrated to bind ice crystals and, hence, were classified as IBPs . The current number of DUF3494 proteins confirmed as IBPs is so large that it raises the question of whether or not there are DUF3494s that do not bind to ice.…”

Section: The Duf3494 Protein Familymentioning

confidence: 99%

“…A) being the most representative (~ 68%). Almost all characterized DUF3494 IBPs exhibit this simple architecture . Generally, single‐DUF3494 IBPs also contain an N‐terminal signal peptide, suggesting that these proteins are secreted into the environment near the cells or accumulate in the membrane .…”

Section: Architecture Of Duf3494 Ibpsmentioning

confidence: 99%

See 1 more Smart Citation

Ice‐binding proteins and the ‘domain of unknown function’ 3494 family

et al. 2019

Self Cite

View full text Add to dashboard Cite

Ice‐binding proteins (IBPs) control the growth and shape of ice crystals to cope with subzero temperatures in psychrophilic and freeze‐tolerant organisms. Recently, numerous proteins containing the domain of unknown function (DUF) 3494 were found to bind ice crystals and, hence, are classified as IBPs. DUF3494 IBPs constitute today the most widespread of the known IBP families. They can be found in different organisms including bacteria, yeasts and microalgae, supporting the hypothesis of horizontal transfer of its gene. Although the 3D structure is always a discontinuous β‐solenoid with a triangular cross‐section and an adjacent alpha‐helix, DUF3494 IBPs present very diverse activities in terms of the magnitude of their thermal hysteresis and inhibition of ice recrystallization. The proteins are secreted into the environments around the host cells or are anchored on their cell membranes. This review covers several aspects of this new class of IBPs, which promise to leave their mark on several research fields including structural biology, protein biochemistry and cryobiology.

show abstract