ArticleProceedings of the National Academy of Sciences of the United States of America2015
Flies expand the repertoire of protein structures that bind ice.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 33 citations in OpenAlex.
- On the engulfment of antifreeze proteins by ice.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Water-organizing motif continuity is critical for potent ice nucleation protein activity.Nature communications · 2022Article
- From ice-binding proteins to bio-inspired antifreeze materials.Soft matter · 2017Review
- Identification of Plant Ice-binding Proteins Through Assessment of Ice-recrystallization Inhibition and Isolation Using Ice-affinity Purification.Journal of visualized experiments : JoVE · 2017Article
- Concentration-dependent oligomerization of an alpha-helical antifreeze polypeptide makes it hyperactive.Scientific reports · 2017Article
- Microfluidic Cold-Finger Device for the Investigation of Ice-Binding Proteins.Biophysical journal · 2016Article
- Modeling repetitive, non-globular proteins.Protein science : a publication of the Protein Society · 2016Review
- New Cysteine-Rich Ice-Binding Protein Secreted from Antarctic Microalga, Chloromonas sp.PloS one · 2016Article
- Origins of De Novo Genes in Human and Chimpanzee.PLoS genetics · 2015Article
- Common protein sequence signatures associate with Sclerotinia borealis lifestyle and secretion in fungal pathogens of the Sclerotiniaceae.Frontiers in plant science · 2015Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
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Abstract
An antifreeze protein (AFP) with no known homologs has been identified in Lake Ontario midges (Chironomidae). The midge AFP is expressed as a family of isoforms at low levels in adults, which emerge from fresh water in spring before the threat of freezing temperatures has passed. The 9.1-kDa major isoform derived from a preproprotein precursor is glycosylated and has a 10-residue tandem repeating sequence xxCxGxYCxG, with regularly spaced cysteines, glycines, and tyrosines comprising one-half its 79 residues. Modeling and molecular dynamics predict a tightly wound left-handed solenoid fold in which the cysteines form a disulfide core to brace each of the eight 10-residue coils. The solenoid is reinforced by intrachain hydrogen bonds, side-chain salt bridges, and a row of seven stacked tyrosines on the hydrophobic side that forms the putative ice-binding site. A disulfide core is also a feature of the similar-sized beetle AFP that is a β-helix with seven 12-residue coils and a comparable circular dichroism spectrum. The midge and beetle AFPs are not homologous and their ice-binding sites are radically different, with the latter comprising two parallel arrays of outward-pointing threonines. However, their structural similarities is an amazing example of convergent evolution in different orders of insects to cope with change to a colder climate and provide confirmation about the physical features needed for a protein to bind ice.
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